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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">The structure of KPN03535 (gi|152972051), a novel putative lipoprotein from <italic>Klebsiella pneumoniae</italic>, reveals an OB-fold</title><author><name sortKey="Das, Debanu" sort="Das, Debanu" uniqKey="Das D" first="Debanu" last="Das">Debanu Das</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="b">Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Kozbial, Piotr" sort="Kozbial, Piotr" uniqKey="Kozbial P" first="Piotr" last="Kozbial">Piotr Kozbial</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="c">Program on Bioinformatics and Systems Biology, Burnham Institute for Medical Research, La Jolla, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Han, Gye Won" sort="Han, Gye Won" uniqKey="Han G" first="Gye Won" last="Han">Gye Won Han</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="d">Department of Molecular Biology, The Scripps Research Institute, La Jolla, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Carlton, Dennis" sort="Carlton, Dennis" uniqKey="Carlton D" first="Dennis" last="Carlton">Dennis Carlton</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="d">Department of Molecular Biology, The Scripps Research Institute, La Jolla, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Jaroszewski, Lukasz" sort="Jaroszewski, Lukasz" uniqKey="Jaroszewski L" first="Lukasz" last="Jaroszewski">Lukasz Jaroszewski</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="c">Program on Bioinformatics and Systems Biology, Burnham Institute for Medical Research, La Jolla, California,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="e">Center for Research in Biological Systems, University of California, San Diego, La Jolla, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Abdubek, Polat" sort="Abdubek, Polat" uniqKey="Abdubek P" first="Polat" last="Abdubek">Polat Abdubek</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="f">Protein Sciences Department, Genomics Institute of the Novartis Research Foundation, San Diego, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Astakhova, Tamara" sort="Astakhova, Tamara" uniqKey="Astakhova T" first="Tamara" last="Astakhova">Tamara Astakhova</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="e">Center for Research in Biological Systems, University of California, San Diego, La Jolla, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Axelrod, Herbert L" sort="Axelrod, Herbert L" uniqKey="Axelrod H" first="Herbert L." last="Axelrod">Herbert L. Axelrod</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="b">Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Bakolitsa, Constantina" sort="Bakolitsa, Constantina" uniqKey="Bakolitsa C" first="Constantina" last="Bakolitsa">Constantina Bakolitsa</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="c">Program on Bioinformatics and Systems Biology, Burnham Institute for Medical Research, La Jolla, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Chen, Connie" sort="Chen, Connie" uniqKey="Chen C" first="Connie" last="Chen">Connie Chen</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="f">Protein Sciences Department, Genomics Institute of the Novartis Research Foundation, San Diego, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Chiu, Hsiu Ju" sort="Chiu, Hsiu Ju" uniqKey="Chiu H" first="Hsiu-Ju" last="Chiu">Hsiu-Ju Chiu</name><affiliation><nlm:aff id="b">Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Chiu, Michelle" sort="Chiu, Michelle" uniqKey="Chiu M" first="Michelle" last="Chiu">Michelle Chiu</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="f">Protein Sciences Department, Genomics Institute of the Novartis Research Foundation, San Diego, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Clayton, Thomas" sort="Clayton, Thomas" uniqKey="Clayton T" first="Thomas" last="Clayton">Thomas Clayton</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="d">Department of Molecular Biology, The Scripps Research Institute, La Jolla, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Deller, Marc C" sort="Deller, Marc C" uniqKey="Deller M" first="Marc C." last="Deller">Marc C. Deller</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="d">Department of Molecular Biology, The Scripps Research Institute, La Jolla, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Duan, Lian" sort="Duan, Lian" uniqKey="Duan L" first="Lian" last="Duan">Lian Duan</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="e">Center for Research in Biological Systems, University of California, San Diego, La Jolla, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Ellrott, Kyle" sort="Ellrott, Kyle" uniqKey="Ellrott K" first="Kyle" last="Ellrott">Kyle Ellrott</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="e">Center for Research in Biological Systems, University of California, San Diego, La Jolla, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Elsliger, Marc Andre" sort="Elsliger, Marc Andre" uniqKey="Elsliger M" first="Marc-André" last="Elsliger">Marc-André Elsliger</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="d">Department of Molecular Biology, The Scripps Research Institute, La Jolla, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Ernst, Dustin" sort="Ernst, Dustin" uniqKey="Ernst D" first="Dustin" last="Ernst">Dustin Ernst</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="f">Protein Sciences Department, Genomics Institute of the Novartis Research Foundation, San Diego, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Farr, Carol L" sort="Farr, Carol L" uniqKey="Farr C" first="Carol L." last="Farr">Carol L. Farr</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="d">Department of Molecular Biology, The Scripps Research Institute, La Jolla, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Feuerhelm, Julie" sort="Feuerhelm, Julie" uniqKey="Feuerhelm J" first="Julie" last="Feuerhelm">Julie Feuerhelm</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="f">Protein Sciences Department, Genomics Institute of the Novartis Research Foundation, San Diego, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Grzechnik, Anna" sort="Grzechnik, Anna" uniqKey="Grzechnik A" first="Anna" last="Grzechnik">Anna Grzechnik</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="d">Department of Molecular Biology, The Scripps Research Institute, La Jolla, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Grant, Joanna C" sort="Grant, Joanna C" uniqKey="Grant J" first="Joanna C." last="Grant">Joanna C. Grant</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="f">Protein Sciences Department, Genomics Institute of the Novartis Research Foundation, San Diego, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Jin, Kevin K" sort="Jin, Kevin K" uniqKey="Jin K" first="Kevin K." last="Jin">Kevin K. Jin</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="b">Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Johnson, Hope A" sort="Johnson, Hope A" uniqKey="Johnson H" first="Hope A." last="Johnson">Hope A. Johnson</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="d">Department of Molecular Biology, The Scripps Research Institute, La Jolla, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Klock, Heath E" sort="Klock, Heath E" uniqKey="Klock H" first="Heath E." last="Klock">Heath E. Klock</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="f">Protein Sciences Department, Genomics Institute of the Novartis Research Foundation, San Diego, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Knuth, Mark W" sort="Knuth, Mark W" uniqKey="Knuth M" first="Mark W." last="Knuth">Mark W. Knuth</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="f">Protein Sciences Department, Genomics Institute of the Novartis Research Foundation, San Diego, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Krishna, S Sri" sort="Krishna, S Sri" uniqKey="Krishna S" first="S. Sri" last="Krishna">S. Sri Krishna</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="c">Program on Bioinformatics and Systems Biology, Burnham Institute for Medical Research, La Jolla, California,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="e">Center for Research in Biological Systems, University of California, San Diego, La Jolla, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Kumar, Abhinav" sort="Kumar, Abhinav" uniqKey="Kumar A" first="Abhinav" last="Kumar">Abhinav Kumar</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="b">Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Marciano, David" sort="Marciano, David" uniqKey="Marciano D" first="David" last="Marciano">David Marciano</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="d">Department of Molecular Biology, The Scripps Research Institute, La Jolla, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Mcmullan, Daniel" sort="Mcmullan, Daniel" uniqKey="Mcmullan D" first="Daniel" last="Mcmullan">Daniel Mcmullan</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="f">Protein Sciences Department, Genomics Institute of the Novartis Research Foundation, San Diego, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Miller, Mitchell D" sort="Miller, Mitchell D" uniqKey="Miller M" first="Mitchell D." last="Miller">Mitchell D. Miller</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="b">Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Morse, Andrew T" sort="Morse, Andrew T" uniqKey="Morse A" first="Andrew T." last="Morse">Andrew T. Morse</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="e">Center for Research in Biological Systems, University of California, San Diego, La Jolla, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Nigoghossian, Edward" sort="Nigoghossian, Edward" uniqKey="Nigoghossian E" first="Edward" last="Nigoghossian">Edward Nigoghossian</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="f">Protein Sciences Department, Genomics Institute of the Novartis Research Foundation, San Diego, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Nopakun, Amanda" sort="Nopakun, Amanda" uniqKey="Nopakun A" first="Amanda" last="Nopakun">Amanda Nopakun</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="d">Department of Molecular Biology, The Scripps Research Institute, La Jolla, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Okach, Linda" sort="Okach, Linda" uniqKey="Okach L" first="Linda" last="Okach">Linda Okach</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="f">Protein Sciences Department, Genomics Institute of the Novartis Research Foundation, San Diego, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Oommachen, Silvya" sort="Oommachen, Silvya" uniqKey="Oommachen S" first="Silvya" last="Oommachen">Silvya Oommachen</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="b">Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Paulsen, Jessica" sort="Paulsen, Jessica" uniqKey="Paulsen J" first="Jessica" last="Paulsen">Jessica Paulsen</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="f">Protein Sciences Department, Genomics Institute of the Novartis Research Foundation, San Diego, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Puckett, Christina" sort="Puckett, Christina" uniqKey="Puckett C" first="Christina" last="Puckett">Christina Puckett</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="f">Protein Sciences Department, Genomics Institute of the Novartis Research Foundation, San Diego, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Reyes, Ron" sort="Reyes, Ron" uniqKey="Reyes R" first="Ron" last="Reyes">Ron Reyes</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="b">Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Rife, Christopher L" sort="Rife, Christopher L" uniqKey="Rife C" first="Christopher L." last="Rife">Christopher L. Rife</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="b">Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Sefcovic, Natasha" sort="Sefcovic, Natasha" uniqKey="Sefcovic N" first="Natasha" last="Sefcovic">Natasha Sefcovic</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="c">Program on Bioinformatics and Systems Biology, Burnham Institute for Medical Research, La Jolla, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Tien, Henry J" sort="Tien, Henry J" uniqKey="Tien H" first="Henry J." last="Tien">Henry J. Tien</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="d">Department of Molecular Biology, The Scripps Research Institute, La Jolla, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Trame, Christine B" sort="Trame, Christine B" uniqKey="Trame C" first="Christine B." last="Trame">Christine B. Trame</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="b">Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Van Den Bedem, Henry" sort="Van Den Bedem, Henry" uniqKey="Van Den Bedem H" first="Henry" last="Van Den Bedem">Henry Van Den Bedem</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="b">Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Weekes, Dana" sort="Weekes, Dana" uniqKey="Weekes D" first="Dana" last="Weekes">Dana Weekes</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="c">Program on Bioinformatics and Systems Biology, Burnham Institute for Medical Research, La Jolla, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Wooten, Tiffany" sort="Wooten, Tiffany" uniqKey="Wooten T" first="Tiffany" last="Wooten">Tiffany Wooten</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="f">Protein Sciences Department, Genomics Institute of the Novartis Research Foundation, San Diego, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Xu, Qingping" sort="Xu, Qingping" uniqKey="Xu Q" first="Qingping" last="Xu">Qingping Xu</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="b">Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Hodgson, Keith O" sort="Hodgson, Keith O" uniqKey="Hodgson K" first="Keith O." last="Hodgson">Keith O. Hodgson</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="g">Photon Science, SLAC National Accelerator Laboratory, Menlo Park, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Wooley, John" sort="Wooley, John" uniqKey="Wooley J" first="John" last="Wooley">John Wooley</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="e">Center for Research in Biological Systems, University of California, San Diego, La Jolla, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Deacon, Ashley M" sort="Deacon, Ashley M" uniqKey="Deacon A" first="Ashley M." last="Deacon">Ashley M. Deacon</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="b">Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Godzik, Adam" sort="Godzik, Adam" uniqKey="Godzik A" first="Adam" last="Godzik">Adam Godzik</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="c">Program on Bioinformatics and Systems Biology, Burnham Institute for Medical Research, La Jolla, California,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="e">Center for Research in Biological Systems, University of California, San Diego, La Jolla, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Lesley, Scott A" sort="Lesley, Scott A" uniqKey="Lesley S" first="Scott A." last="Lesley">Scott A. Lesley</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="d">Department of Molecular Biology, The Scripps Research Institute, La Jolla, California,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="f">Protein Sciences Department, Genomics Institute of the Novartis Research Foundation, San Diego, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Wilson, Ian A" sort="Wilson, Ian A" uniqKey="Wilson I" first="Ian A." last="Wilson">Ian A. Wilson</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="d">Department of Molecular Biology, The Scripps Research Institute, La Jolla, California,<country>USA</country></nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">20944219</idno><idno type="pmc">2954213</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2954213</idno><idno type="RBID">PMC:2954213</idno><idno type="doi">10.1107/S1744309109018168</idno><date when="2009">2009</date><idno type="wicri:Area/Pmc/Corpus">000176</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000176</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">The structure of KPN03535 (gi|152972051), a novel putative lipoprotein from <italic>Klebsiella pneumoniae</italic>, reveals an OB-fold</title><author><name sortKey="Das, Debanu" sort="Das, Debanu" uniqKey="Das D" first="Debanu" last="Das">Debanu Das</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="b">Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Kozbial, Piotr" sort="Kozbial, Piotr" uniqKey="Kozbial P" first="Piotr" last="Kozbial">Piotr Kozbial</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="c">Program on Bioinformatics and Systems Biology, Burnham Institute for Medical Research, La Jolla, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Han, Gye Won" sort="Han, Gye Won" uniqKey="Han G" first="Gye Won" last="Han">Gye Won Han</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="d">Department of Molecular Biology, The Scripps Research Institute, La Jolla, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Carlton, Dennis" sort="Carlton, Dennis" uniqKey="Carlton D" first="Dennis" last="Carlton">Dennis Carlton</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="d">Department of Molecular Biology, The Scripps Research Institute, La Jolla, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Jaroszewski, Lukasz" sort="Jaroszewski, Lukasz" uniqKey="Jaroszewski L" first="Lukasz" last="Jaroszewski">Lukasz Jaroszewski</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="c">Program on Bioinformatics and Systems Biology, Burnham Institute for Medical Research, La Jolla, California,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="e">Center for Research in Biological Systems, University of California, San Diego, La Jolla, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Abdubek, Polat" sort="Abdubek, Polat" uniqKey="Abdubek P" first="Polat" last="Abdubek">Polat Abdubek</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="f">Protein Sciences Department, Genomics Institute of the Novartis Research Foundation, San Diego, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Astakhova, Tamara" sort="Astakhova, Tamara" uniqKey="Astakhova T" first="Tamara" last="Astakhova">Tamara Astakhova</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="e">Center for Research in Biological Systems, University of California, San Diego, La Jolla, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Axelrod, Herbert L" sort="Axelrod, Herbert L" uniqKey="Axelrod H" first="Herbert L." last="Axelrod">Herbert L. Axelrod</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="b">Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Bakolitsa, Constantina" sort="Bakolitsa, Constantina" uniqKey="Bakolitsa C" first="Constantina" last="Bakolitsa">Constantina Bakolitsa</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="c">Program on Bioinformatics and Systems Biology, Burnham Institute for Medical Research, La Jolla, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Chen, Connie" sort="Chen, Connie" uniqKey="Chen C" first="Connie" last="Chen">Connie Chen</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="f">Protein Sciences Department, Genomics Institute of the Novartis Research Foundation, San Diego, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Chiu, Hsiu Ju" sort="Chiu, Hsiu Ju" uniqKey="Chiu H" first="Hsiu-Ju" last="Chiu">Hsiu-Ju Chiu</name><affiliation><nlm:aff id="b">Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Chiu, Michelle" sort="Chiu, Michelle" uniqKey="Chiu M" first="Michelle" last="Chiu">Michelle Chiu</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="f">Protein Sciences Department, Genomics Institute of the Novartis Research Foundation, San Diego, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Clayton, Thomas" sort="Clayton, Thomas" uniqKey="Clayton T" first="Thomas" last="Clayton">Thomas Clayton</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="d">Department of Molecular Biology, The Scripps Research Institute, La Jolla, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Deller, Marc C" sort="Deller, Marc C" uniqKey="Deller M" first="Marc C." last="Deller">Marc C. Deller</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="d">Department of Molecular Biology, The Scripps Research Institute, La Jolla, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Duan, Lian" sort="Duan, Lian" uniqKey="Duan L" first="Lian" last="Duan">Lian Duan</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="e">Center for Research in Biological Systems, University of California, San Diego, La Jolla, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Ellrott, Kyle" sort="Ellrott, Kyle" uniqKey="Ellrott K" first="Kyle" last="Ellrott">Kyle Ellrott</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="e">Center for Research in Biological Systems, University of California, San Diego, La Jolla, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Elsliger, Marc Andre" sort="Elsliger, Marc Andre" uniqKey="Elsliger M" first="Marc-André" last="Elsliger">Marc-André Elsliger</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="d">Department of Molecular Biology, The Scripps Research Institute, La Jolla, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Ernst, Dustin" sort="Ernst, Dustin" uniqKey="Ernst D" first="Dustin" last="Ernst">Dustin Ernst</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="f">Protein Sciences Department, Genomics Institute of the Novartis Research Foundation, San Diego, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Farr, Carol L" sort="Farr, Carol L" uniqKey="Farr C" first="Carol L." last="Farr">Carol L. Farr</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="d">Department of Molecular Biology, The Scripps Research Institute, La Jolla, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Feuerhelm, Julie" sort="Feuerhelm, Julie" uniqKey="Feuerhelm J" first="Julie" last="Feuerhelm">Julie Feuerhelm</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="f">Protein Sciences Department, Genomics Institute of the Novartis Research Foundation, San Diego, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Grzechnik, Anna" sort="Grzechnik, Anna" uniqKey="Grzechnik A" first="Anna" last="Grzechnik">Anna Grzechnik</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="d">Department of Molecular Biology, The Scripps Research Institute, La Jolla, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Grant, Joanna C" sort="Grant, Joanna C" uniqKey="Grant J" first="Joanna C." last="Grant">Joanna C. Grant</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="f">Protein Sciences Department, Genomics Institute of the Novartis Research Foundation, San Diego, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Jin, Kevin K" sort="Jin, Kevin K" uniqKey="Jin K" first="Kevin K." last="Jin">Kevin K. Jin</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="b">Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Johnson, Hope A" sort="Johnson, Hope A" uniqKey="Johnson H" first="Hope A." last="Johnson">Hope A. Johnson</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="d">Department of Molecular Biology, The Scripps Research Institute, La Jolla, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Klock, Heath E" sort="Klock, Heath E" uniqKey="Klock H" first="Heath E." last="Klock">Heath E. Klock</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="f">Protein Sciences Department, Genomics Institute of the Novartis Research Foundation, San Diego, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Knuth, Mark W" sort="Knuth, Mark W" uniqKey="Knuth M" first="Mark W." last="Knuth">Mark W. Knuth</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="f">Protein Sciences Department, Genomics Institute of the Novartis Research Foundation, San Diego, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Krishna, S Sri" sort="Krishna, S Sri" uniqKey="Krishna S" first="S. Sri" last="Krishna">S. Sri Krishna</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="c">Program on Bioinformatics and Systems Biology, Burnham Institute for Medical Research, La Jolla, California,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="e">Center for Research in Biological Systems, University of California, San Diego, La Jolla, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Kumar, Abhinav" sort="Kumar, Abhinav" uniqKey="Kumar A" first="Abhinav" last="Kumar">Abhinav Kumar</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="b">Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Marciano, David" sort="Marciano, David" uniqKey="Marciano D" first="David" last="Marciano">David Marciano</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="d">Department of Molecular Biology, The Scripps Research Institute, La Jolla, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Mcmullan, Daniel" sort="Mcmullan, Daniel" uniqKey="Mcmullan D" first="Daniel" last="Mcmullan">Daniel Mcmullan</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="f">Protein Sciences Department, Genomics Institute of the Novartis Research Foundation, San Diego, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Miller, Mitchell D" sort="Miller, Mitchell D" uniqKey="Miller M" first="Mitchell D." last="Miller">Mitchell D. Miller</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="b">Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Morse, Andrew T" sort="Morse, Andrew T" uniqKey="Morse A" first="Andrew T." last="Morse">Andrew T. Morse</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="e">Center for Research in Biological Systems, University of California, San Diego, La Jolla, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Nigoghossian, Edward" sort="Nigoghossian, Edward" uniqKey="Nigoghossian E" first="Edward" last="Nigoghossian">Edward Nigoghossian</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="f">Protein Sciences Department, Genomics Institute of the Novartis Research Foundation, San Diego, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Nopakun, Amanda" sort="Nopakun, Amanda" uniqKey="Nopakun A" first="Amanda" last="Nopakun">Amanda Nopakun</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="d">Department of Molecular Biology, The Scripps Research Institute, La Jolla, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Okach, Linda" sort="Okach, Linda" uniqKey="Okach L" first="Linda" last="Okach">Linda Okach</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="f">Protein Sciences Department, Genomics Institute of the Novartis Research Foundation, San Diego, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Oommachen, Silvya" sort="Oommachen, Silvya" uniqKey="Oommachen S" first="Silvya" last="Oommachen">Silvya Oommachen</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="b">Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Paulsen, Jessica" sort="Paulsen, Jessica" uniqKey="Paulsen J" first="Jessica" last="Paulsen">Jessica Paulsen</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="f">Protein Sciences Department, Genomics Institute of the Novartis Research Foundation, San Diego, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Puckett, Christina" sort="Puckett, Christina" uniqKey="Puckett C" first="Christina" last="Puckett">Christina Puckett</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="f">Protein Sciences Department, Genomics Institute of the Novartis Research Foundation, San Diego, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Reyes, Ron" sort="Reyes, Ron" uniqKey="Reyes R" first="Ron" last="Reyes">Ron Reyes</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="b">Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Rife, Christopher L" sort="Rife, Christopher L" uniqKey="Rife C" first="Christopher L." last="Rife">Christopher L. Rife</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="b">Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Sefcovic, Natasha" sort="Sefcovic, Natasha" uniqKey="Sefcovic N" first="Natasha" last="Sefcovic">Natasha Sefcovic</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="c">Program on Bioinformatics and Systems Biology, Burnham Institute for Medical Research, La Jolla, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Tien, Henry J" sort="Tien, Henry J" uniqKey="Tien H" first="Henry J." last="Tien">Henry J. Tien</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="d">Department of Molecular Biology, The Scripps Research Institute, La Jolla, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Trame, Christine B" sort="Trame, Christine B" uniqKey="Trame C" first="Christine B." last="Trame">Christine B. Trame</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="b">Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Van Den Bedem, Henry" sort="Van Den Bedem, Henry" uniqKey="Van Den Bedem H" first="Henry" last="Van Den Bedem">Henry Van Den Bedem</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="b">Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Weekes, Dana" sort="Weekes, Dana" uniqKey="Weekes D" first="Dana" last="Weekes">Dana Weekes</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="c">Program on Bioinformatics and Systems Biology, Burnham Institute for Medical Research, La Jolla, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Wooten, Tiffany" sort="Wooten, Tiffany" uniqKey="Wooten T" first="Tiffany" last="Wooten">Tiffany Wooten</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="f">Protein Sciences Department, Genomics Institute of the Novartis Research Foundation, San Diego, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Xu, Qingping" sort="Xu, Qingping" uniqKey="Xu Q" first="Qingping" last="Xu">Qingping Xu</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="b">Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Hodgson, Keith O" sort="Hodgson, Keith O" uniqKey="Hodgson K" first="Keith O." last="Hodgson">Keith O. Hodgson</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="g">Photon Science, SLAC National Accelerator Laboratory, Menlo Park, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Wooley, John" sort="Wooley, John" uniqKey="Wooley J" first="John" last="Wooley">John Wooley</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="e">Center for Research in Biological Systems, University of California, San Diego, La Jolla, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Deacon, Ashley M" sort="Deacon, Ashley M" uniqKey="Deacon A" first="Ashley M." last="Deacon">Ashley M. Deacon</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="b">Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Godzik, Adam" sort="Godzik, Adam" uniqKey="Godzik A" first="Adam" last="Godzik">Adam Godzik</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="c">Program on Bioinformatics and Systems Biology, Burnham Institute for Medical Research, La Jolla, California,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="e">Center for Research in Biological Systems, University of California, San Diego, La Jolla, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Lesley, Scott A" sort="Lesley, Scott A" uniqKey="Lesley S" first="Scott A." last="Lesley">Scott A. Lesley</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="d">Department of Molecular Biology, The Scripps Research Institute, La Jolla, California,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="f">Protein Sciences Department, Genomics Institute of the Novartis Research Foundation, San Diego, California,<country>USA</country></nlm:aff></affiliation></author><author><name sortKey="Wilson, Ian A" sort="Wilson, Ian A" uniqKey="Wilson I" first="Ian A." last="Wilson">Ian A. Wilson</name><affiliation><nlm:aff id="a">Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></nlm:aff></affiliation><affiliation><nlm:aff id="d">Department of Molecular Biology, The Scripps Research Institute, La Jolla, California,<country>USA</country></nlm:aff></affiliation></author></analytic><series><title level="j">Acta Crystallographica Section F: Structural Biology and Crystallization Communications</title><idno type="eISSN">1744-3091</idno><imprint><date when="2009">2009</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>KPN03535 is a protein unique to <italic>K. pneumoniae</italic>. The crystal structure reveals that KPN03535 represents a novel variant of the OB-fold and is likely to be a DNA-binding lipoprotein.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct></listBibl></div1></back></TEI><pmc article-type="research-article"><pmc-dir>properties open_access</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Acta Crystallogr Sect F Struct Biol Cryst Commun</journal-id><journal-id journal-id-type="publisher-id">Acta Cryst. F</journal-id><journal-title-group><journal-title>Acta Crystallographica Section F: Structural Biology and Crystallization Communications</journal-title></journal-title-group><issn pub-type="epub">1744-3091</issn><publisher><publisher-name>International Union of Crystallography</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">20944219</article-id><article-id pub-id-type="pmc">2954213</article-id><article-id pub-id-type="publisher-id">wd5110</article-id><article-id pub-id-type="doi">10.1107/S1744309109018168</article-id><article-id pub-id-type="coden">ACSFCL</article-id><article-id pub-id-type="pii">S1744309109018168</article-id><article-categories><subj-group subj-group-type="heading"><subject>Novel Variants of Known Folds and Function</subject></subj-group></article-categories><title-group><article-title>The structure of KPN03535 (gi|152972051), a novel putative lipoprotein from <italic>Klebsiella pneumoniae</italic>, reveals an 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contrib-type="author"><name><surname>Knuth</surname><given-names>Mark W.</given-names></name><xref ref-type="aff" rid="a">a</xref><xref ref-type="aff" rid="f">f</xref></contrib><contrib contrib-type="author"><name><surname>Krishna</surname><given-names>S. Sri</given-names></name><xref ref-type="aff" rid="a">a</xref><xref ref-type="aff" rid="c">c</xref><xref ref-type="aff" rid="e">e</xref></contrib><contrib contrib-type="author"><name><surname>Kumar</surname><given-names>Abhinav</given-names></name><xref ref-type="aff" rid="a">a</xref><xref ref-type="aff" rid="b">b</xref></contrib><contrib contrib-type="author"><name><surname>Marciano</surname><given-names>David</given-names></name><xref ref-type="aff" rid="a">a</xref><xref ref-type="aff" rid="d">d</xref></contrib><contrib contrib-type="author"><name><surname>McMullan</surname><given-names>Daniel</given-names></name><xref ref-type="aff" rid="a">a</xref><xref ref-type="aff" rid="f">f</xref></contrib><contrib contrib-type="author"><name><surname>Miller</surname><given-names>Mitchell D.</given-names></name><xref ref-type="aff" rid="a">a</xref><xref ref-type="aff" rid="b">b</xref></contrib><contrib contrib-type="author"><name><surname>Morse</surname><given-names>Andrew T.</given-names></name><xref ref-type="aff" rid="a">a</xref><xref ref-type="aff" rid="e">e</xref></contrib><contrib contrib-type="author"><name><surname>Nigoghossian</surname><given-names>Edward</given-names></name><xref ref-type="aff" rid="a">a</xref><xref ref-type="aff" rid="f">f</xref></contrib><contrib contrib-type="author"><name><surname>Nopakun</surname><given-names>Amanda</given-names></name><xref ref-type="aff" rid="a">a</xref><xref ref-type="aff" rid="d">d</xref></contrib><contrib contrib-type="author"><name><surname>Okach</surname><given-names>Linda</given-names></name><xref ref-type="aff" rid="a">a</xref><xref ref-type="aff" rid="f">f</xref></contrib><contrib contrib-type="author"><name><surname>Oommachen</surname><given-names>Silvya</given-names></name><xref ref-type="aff" rid="a">a</xref><xref ref-type="aff" rid="b">b</xref></contrib><contrib contrib-type="author"><name><surname>Paulsen</surname><given-names>Jessica</given-names></name><xref ref-type="aff" rid="a">a</xref><xref ref-type="aff" rid="f">f</xref></contrib><contrib contrib-type="author"><name><surname>Puckett</surname><given-names>Christina</given-names></name><xref ref-type="aff" rid="a">a</xref><xref ref-type="aff" rid="f">f</xref></contrib><contrib contrib-type="author"><name><surname>Reyes</surname><given-names>Ron</given-names></name><xref ref-type="aff" rid="a">a</xref><xref ref-type="aff" rid="b">b</xref></contrib><contrib contrib-type="author"><name><surname>Rife</surname><given-names>Christopher L.</given-names></name><xref ref-type="aff" rid="a">a</xref><xref ref-type="aff" rid="b">b</xref></contrib><contrib contrib-type="author"><name><surname>Sefcovic</surname><given-names>Natasha</given-names></name><xref ref-type="aff" rid="a">a</xref><xref ref-type="aff" rid="c">c</xref></contrib><contrib contrib-type="author"><name><surname>Tien</surname><given-names>Henry J.</given-names></name><xref ref-type="aff" rid="a">a</xref><xref ref-type="aff" rid="d">d</xref></contrib><contrib contrib-type="author"><name><surname>Trame</surname><given-names>Christine B.</given-names></name><xref ref-type="aff" rid="a">a</xref><xref ref-type="aff" rid="b">b</xref></contrib><contrib contrib-type="author"><name><surname>van den Bedem</surname><given-names>Henry</given-names></name><xref ref-type="aff" rid="a">a</xref><xref ref-type="aff" rid="b">b</xref></contrib><contrib contrib-type="author"><name><surname>Weekes</surname><given-names>Dana</given-names></name><xref ref-type="aff" rid="a">a</xref><xref ref-type="aff" rid="c">c</xref></contrib><contrib contrib-type="author"><name><surname>Wooten</surname><given-names>Tiffany</given-names></name><xref ref-type="aff" rid="a">a</xref><xref ref-type="aff" rid="f">f</xref></contrib><contrib contrib-type="author"><name><surname>Xu</surname><given-names>Qingping</given-names></name><xref ref-type="aff" rid="a">a</xref><xref ref-type="aff" rid="b">b</xref></contrib><contrib contrib-type="author"><name><surname>Hodgson</surname><given-names>Keith O.</given-names></name><xref ref-type="aff" rid="a">a</xref><xref ref-type="aff" rid="g">g</xref></contrib><contrib contrib-type="author"><name><surname>Wooley</surname><given-names>John</given-names></name><xref ref-type="aff" rid="a">a</xref><xref ref-type="aff" rid="e">e</xref></contrib><contrib contrib-type="author"><name><surname>Deacon</surname><given-names>Ashley M.</given-names></name><xref ref-type="aff" rid="a">a</xref><xref ref-type="aff" rid="b">b</xref></contrib><contrib contrib-type="author"><name><surname>Godzik</surname><given-names>Adam</given-names></name><xref ref-type="aff" rid="a">a</xref><xref ref-type="aff" rid="c">c</xref><xref ref-type="aff" rid="e">e</xref></contrib><contrib contrib-type="author"><name><surname>Lesley</surname><given-names>Scott A.</given-names></name><xref ref-type="aff" rid="a">a</xref><xref ref-type="aff" rid="d">d</xref><xref ref-type="aff" rid="f">f</xref></contrib><contrib contrib-type="author"><name><surname>Wilson</surname><given-names>Ian A.</given-names></name><xref ref-type="aff" rid="a">a</xref><xref ref-type="aff" rid="d">d</xref><xref ref-type="corresp" rid="cor">*</xref></contrib><aff id="a"><label>a</label>Joint Center for Structural Genomics,<ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>,<country>USA</country></aff><aff id="b"><label>b</label>Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, California,<country>USA</country></aff><aff id="c"><label>c</label>Program on Bioinformatics and Systems Biology, Burnham Institute for Medical Research, La Jolla, California,<country>USA</country></aff><aff id="d"><label>d</label>Department of Molecular Biology, The Scripps Research Institute, La Jolla, California,<country>USA</country></aff><aff id="e"><label>e</label>Center for Research in Biological Systems, University of California, San Diego, La Jolla, California,<country>USA</country></aff><aff id="f"><label>f</label>Protein Sciences Department, Genomics Institute of the Novartis Research Foundation, San Diego, California,<country>USA</country></aff><aff id="g"><label>g</label>Photon Science, SLAC National Accelerator Laboratory, Menlo Park, California,<country>USA</country></aff></contrib-group><author-notes><corresp id="cor">Correspondence e-mail: <email>wilson@scripps.edu</email></corresp></author-notes><pub-date pub-type="collection"><day>1</day><month>10</month><year>2010</year></pub-date><pub-date pub-type="epub"><day>27</day><month>10</month><year>2009</year></pub-date><pub-date pub-type="pmc-release"><day>27</day><month>10</month><year>2009</year></pub-date><pmc-comment> PMC Release delay is 0 months and 0 days and was based on the
<volume>66</volume><issue>Pt 10</issue><issue-id pub-id-type="publisher-id">f101000</issue-id><fpage>1254</fpage><lpage>1260</lpage><history><date date-type="received"><day>16</day><month>4</month><year>2009</year></date><date date-type="accepted"><day>13</day><month>5</month><year>2009</year></date></history><permissions><copyright-statement>© Das et al. 2010</copyright-statement><copyright-year>2010</copyright-year><license license-type="open-access" xlink:href="http://creativecommons.org/licenses/by/2.0/uk/"><license-p>This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.</license-p></license></permissions><self-uri xlink:type="simple" xlink:href="http://dx.doi.org/10.1107/S1744309109018168">A full version of this article is available from Crystallography Journals Online.</self-uri><abstract abstract-type="toc"><p>KPN03535 is a protein unique to <italic>K. pneumoniae</italic>. The crystal structure reveals that KPN03535 represents a novel variant of the OB-fold and is likely to be a DNA-binding lipoprotein.</p></abstract><abstract><p>KPN03535 (gi|152972051) is a putative lipoprotein of unknown function that is secreted by <italic>Klebsiella pneumoniae</italic> MGH 78578. The crystal structure reveals that despite a lack of any detectable sequence similarity to known structures, it is a novel variant of the OB-fold and structurally similar to the bacterial Cpx-pathway protein NlpE, single-stranded DNA-binding (SSB) proteins and toxins. <italic>K. pneumoniae</italic> MGH 78578 forms part of the normal human skin, mouth and gut flora and is an opportunistic pathogen that is linked to about 8% of all hospital-acquired infections in the USA. This structure provides the foundation for further investigations into this divergent member of the OB-fold family.</p></abstract><kwd-group><kwd>lipoproteins</kwd><kwd>OB-fold</kwd><kwd>NipE-like protein</kwd><kwd>single-stranded DNA-binding proteins</kwd><kwd>toxins</kwd><kwd>BOF</kwd><kwd>human gut pathogens</kwd><kwd>structural genomics</kwd></kwd-group><conference><conf-date></conf-date><conf-name>Joint Center for Structural Genomics (JCSG) special issue</conf-name><conf-loc></conf-loc></conference></article-meta></front><body><sec sec-type="introduction" id="sec1"><label>1.</label><title>Introduction</title><p>KPN03535 (gi|152972051) is an orphan protein that is exclusively found in <italic>Klebsiella pneumoniae</italic> MGH 78578 (an opportunistic human pathogen belonging to enterbacteriales of gammaproteobacteria; Galperin <italic>et al.</italic>, 2007<xref ref-type="bibr" rid="bb65"> ▶</xref>; Gill <italic>et al.</italic>, 2006<xref ref-type="bibr" rid="bb15"> ▶</xref>; Frank & Pace, 2008<xref ref-type="bibr" rid="bb13"> ▶</xref>; Ley <italic>et al.</italic>, 2008<xref ref-type="bibr" rid="bb33"> ▶</xref>) and <italic>K. pneumoniae</italic> 342 (three-residue substitution). It consists of 132 residues with a calculated pI of 9.40 and a predicted signal peptide. The N-terminus of KPN03535 has a lipoprotein signature, indicated by the presence of an LSGC motif (von Heijne, 1989<xref ref-type="bibr" rid="bb18"> ▶</xref>), as well as predictions from <italic>LipoP</italic> 1.0 (Juncker <italic>et al.</italic>, 2003<xref ref-type="bibr" rid="bb24"> ▶</xref>). It is a singleton protein that has not been assigned to any Pfam family, but sequence-based fold-prediction methods (Ginalski <italic>et al.</italic>, 2003<xref ref-type="bibr" rid="bb16"> ▶</xref>) suggest similarity to members of the PF01336 family (OB-fold nucleic acid-binding domain). We determined the crystal structure of KPN03535 in order to explore this extremely divergent member of the commonly occurring OB-fold. Structural comparisons show similarities to the OB-fold-containing Cpx-pathway protein NlpE, single-stranded DNA-binding (SSB) proteins, bacterial OB-fold (BOF) and toxin proteins, which enable inferences about function that may now be tested biochemically. This structure should serve as a basis for understanding structure–function relationships in any newly discovered proteins with a similar sequence, such as those identified by whole microbial genome sequencing and metagenomic surveys of the human microbiome.</p></sec><sec sec-type="materials|methods" id="sec2"><label>2.</label><title>Materials and methods</title><sec id="sec2.1"><label>2.1.</label><title>KPN03535 expression, purification and crystallization</title><p>Clones were generated using the Polymerase Incomplete Primer Extension (PIPE; Klock <italic>et al.</italic>, 2008<xref ref-type="bibr" rid="bb26"> ▶</xref>) cloning method. The gene encoding KPN03535 (gi|152972051; Swiss-Prot A6TEE6) was amplified by polymerase chain reaction (PCR) from <italic>K. pneumoniae</italic> MGH 78578 genomic DNA using <italic>PfuTurbo</italic> DNA polymerase (Stratagene) and I-PIPE (Insert) primers (forward primer, 5′-ctgtacttccagggcGCTTCTAAAGCCTTTTATTCCGCGGGAG-3′; reverse primer, 5′-aattaagtcgcgttaTTTAACCACCTTGGGATTCTGTAGCGTC-3′; target sequence in upper case) that included sequences for the predicted 5′- and 3′-ends. The expression vector, pSpeedET, which encodes an amino-terminal tobacco etch virus (TEV) protease-cleavable expression and purification tag (MGSDKIHHHHHHENLYFQG), was PCR-amplified with V-PIPE (Vector) primers (forward primer, 5′-taacgcgacttaattaactcgtttaaacggtctccagc-3′; reverse primer, 5′-gccctggaagtacaggttttcgtgatgatgatgatgatg-3′). V-PIPE and I-PIPE PCR products were mixed to anneal the amplified DNA fragments together. <italic>Escherichia coli</italic> GeneHogs (Invitrogen) competent cells were transformed with the V-PIPE/I-PIPE mixture and dispensed on selective LB-agar plates. The cloning junctions were confirmed by DNA sequencing. Using the PIPE method, the gene segment encoding residues Met1–Leu22 was deleted for expression of soluble protein as these residues were initially predicted to correspond to either a signal peptide using <italic>SignalP</italic> (Bendtsen <italic>et al.</italic>, 2004<xref ref-type="bibr" rid="bb1"> ▶</xref>) or transmembrane helices using <italic>TMHMM</italic>-2.0 (Krogh <italic>et al.</italic>, 2001<xref ref-type="bibr" rid="bb29"> ▶</xref>). Expression was performed in selenomethionine-containing medium. At the end of fermentation, lysozyme was added to the culture to a final concentration of 250 µg ml<sup>−1</sup> and the cells were harvested and frozen. After one freeze–thaw cycle, the cells were homogenized in lysis buffer [50 m<italic>M</italic> HEPES pH 8.0, 50 m<italic>M</italic> NaCl, 10 m<italic>M</italic> imidazole, 1 m<italic>M</italic> tris(2-carboxyethyl)phosphine–HCl (TCEP)] and the lysate was clarified by centrifugation at 32 500<italic>g</italic> for 30 min. The soluble fraction was passed over nickel-chelating resin (GE Healthcare) pre-equilibrated with lysis buffer, the resin was washed with wash buffer [50 m<italic>M</italic> HEPES pH 8.0, 300 m<italic>M</italic> NaCl, 40 m<italic>M</italic> imidazole, 10%(<italic>v</italic>/<italic>v</italic>) glycerol, 1 m<italic>M</italic> TCEP] and the protein was eluted with elution buffer [20 m<italic>M</italic> HEPES pH 8.0, 300 m<italic>M</italic> imidazole, 10%(<italic>v</italic>/<italic>v</italic>) glycerol, 1 m<italic>M</italic> TCEP]. The eluate was buffer-exchanged with TEV buffer (20 m<italic>M</italic> HEPES pH 8.0, 200 m<italic>M</italic> NaCl, 40 m<italic>M</italic> imidazole, 1 m<italic>M</italic> TCEP) using a PD-10 column (GE Healthcare) and incubated with 1 mg TEV protease per 15 mg of eluted protein. The protease-treated eluate was passed over nickel-chelating resin (GE Healthcare) pre-equilibrated with HEPES crystallization buffer (20 m<italic>M</italic> HEPES pH 8.0, 200 m<italic>M</italic> NaCl, 40 m<italic>M</italic> imidazole, 1 m<italic>M</italic> TCEP) and the resin was washed with the same buffer. The flowthrough and wash fractions were combined and concentrated for crystallization trials to 16.1 mg ml<sup>−1</sup> by centrifugal ultrafiltration (Millipore). KPN03535 was crystallized by mixing 100 nl protein solution with 100 nl crystallization solution in a sitting drop over a 50 µl reservoir volume using the nanodroplet vapor-diffusion method (Santarsiero <italic>et al.</italic>, 2002<xref ref-type="bibr" rid="bb47"> ▶</xref>) with standard Joint Center for Structural Genomics (JCSG; <ext-link ext-link-type="uri" xlink:href="http://www.jcsg.org">http://www.jcsg.org</ext-link>) crystallization protocols (Lesley <italic>et al.</italic>, 2002<xref ref-type="bibr" rid="bb31"> ▶</xref>). The crystallization reagent contained 31% polyethylene glycol 600 and 0.1 <italic>M</italic> CHES pH 9.5. No further cryoprotectant was added to the crystal. A cube-shaped crystal with approximate dimensions 80 × 80 × 80 µm was harvested after 42 d at 293 K for data collection. Initial screening for diffraction was carried out using the Stanford Automated Mounting system (SAM; Cohen <italic>et al.</italic>, 2002<xref ref-type="bibr" rid="bb3"> ▶</xref>) at the Stanford Synchrotron Radiation Lightsource (SSRL; Menlo Park, California, USA). The diffraction data were indexed in the orthorhombic space group <italic>P</italic>2<sub>1</sub>2<sub>1</sub>2<sub>1</sub>. The molecular weight and oligomeric state were determined using a 1 × 30 cm Superdex 200 column (GE Healthcare) in combination with static light scattering (Wyatt Technology). The mobile phase consisted of 20 m<italic>M</italic> Tris pH 8.0, 150 m<italic>M</italic> NaCl and 0.02%(<italic>w</italic>/<italic>v</italic>) sodium azide.</p></sec><sec id="sec2.2"><label>2.2.</label><title>X-ray data collection and structure determination</title><p>Single-wavelength anomalous diffraction (SAD) data were collected to 2.46 Å resolution on beamline 9-2 at SSRL at the wavelength corresponding to the peak (λ<sub>1</sub>) of a selenium absorption edge using the <italic>Blu-Ice</italic> data-collection environment (McPhillips <italic>et al.</italic>, 2002<xref ref-type="bibr" rid="bb38"> ▶</xref>). A data set was collected at 100 K using a MAR Mosaic 325 CCD detector (Rayonix USA). The SAD data were integrated and reduced using <italic>MOSFLM</italic> (Leslie, 1992<xref ref-type="bibr" rid="bb32"> ▶</xref>) and scaled with the program <italic>SCALA</italic> (Collaborative Computational Project, Number 4, 1994<xref ref-type="bibr" rid="bb4"> ▶</xref>). Phasing was performed with <italic>SHELXD</italic> (Sheldrick, 2008<xref ref-type="bibr" rid="bb48"> ▶</xref>) and <italic>autoSHARP</italic> (Vonrhein <italic>et al.</italic>, 2007<xref ref-type="bibr" rid="bb57"> ▶</xref>) [20 selenium sites per asymmetric unit, overall FOM (acentric/centric) = 0.34/0.12, overall phasing power (anomalous differences) = 1.2] and automated iterative model building was performed with <italic>RESOLVE</italic> (Terwilliger, 2003<xref ref-type="bibr" rid="bb52"> ▶</xref>). Model completion and crystallographic refinement were performed with <italic>Coot</italic> (Emsley & Cowtan, 2004<xref ref-type="bibr" rid="bb12"> ▶</xref>) and <italic>REFMAC</italic>5 (Collaborative Computational Project, Number 4, 1994<xref ref-type="bibr" rid="bb4"> ▶</xref>) with TLS (one group per monomer) refinement (Winn <italic>et al.</italic>, 2003<xref ref-type="bibr" rid="bb59"> ▶</xref>) and medium NCS restraints for all chains. Data and refinement statistics are summarized in Table 1<xref ref-type="table" rid="table1"> ▶</xref>.</p><p>The quality of the crystal structure was analyzed using the JCSG Quality Control server, which verifies the stereochemical quality of the model using <italic>AutoDepInputTool</italic> (Yang <italic>et al.</italic>, 2004<xref ref-type="bibr" rid="bb62"> ▶</xref>), <italic>MolProbity</italic> (Davis <italic>et al.</italic>, 2004<xref ref-type="bibr" rid="bb9"> ▶</xref>) and <italic>WHATIF</italic> 5.0 (Vriend, 1990<xref ref-type="bibr" rid="bb58"> ▶</xref>), the agreement between the atomic model and the data using <italic>SFCHECK</italic> 4.0 (Vaguine <italic>et al.</italic>, 1999<xref ref-type="bibr" rid="bb56"> ▶</xref>) and <italic>RESOLVE</italic> (Terwilliger, 2000<xref ref-type="bibr" rid="bb51"> ▶</xref>), the protein sequence using <italic>ClustalW</italic> (Thompson <italic>et al.</italic>, 1994<xref ref-type="bibr" rid="bb54"> ▶</xref>), atom occupancies using <italic>MOLEMAN</italic>2 (Kleywegt, 2000<xref ref-type="bibr" rid="bb25"> ▶</xref>) and the consistency of NCS pairs. This analysis also evaluates difference in <italic>R</italic><sub>cryst</sub>/<italic>R</italic><sub>free</sub>, expected <italic>R</italic><sub>free</sub>/<italic>R</italic><sub>cryst</sub> and maximum/minimum <italic>B</italic> values by parsing the refinement log-file and PDB header. Protein quaternary structure analysis was performed using the <italic>PISA</italic> server (Krissinel & Henrick, 2005<xref ref-type="bibr" rid="bb28"> ▶</xref>). Fig. 1<xref ref-type="fig" rid="fig1"> ▶</xref>(<italic>b</italic>) was adapted from an analysis using <italic>PDBsum</italic> (Laskowski <italic>et al.</italic>, 2005<xref ref-type="bibr" rid="bb30"> ▶</xref>) and all other figures were prepared with <italic>PyMOL</italic> (DeLano, 2002<xref ref-type="bibr" rid="bb10"> ▶</xref>). Atomic coordinates and experimental structure factors for KPN03535 have been deposited in the PDB under accession code <ext-link ext-link-type="uri" xlink:href="http://scripts.iucr.org/cgi-bin/cr.cgi?rm=pdb&pdbId=3f1z">3f1z</ext-link>. A systematic search for other proteins of similar structure was conducted using several different methods including the <italic>DALI</italic> server (Holm <italic>et al.</italic>, 2008<xref ref-type="bibr" rid="bb21"> ▶</xref>), the protein structure comparison service <italic>SSM</italic> at the European Bioinformatics Institute (<ext-link ext-link-type="uri" xlink:href="http://www.ebi.ac.uk/msd-srv/ssm">http://www.ebi.ac.uk/msd-srv/ssm</ext-link>; Krissinel & Henrick, 2004<xref ref-type="bibr" rid="bb27"> ▶</xref>) and the flexible structure-alignment method <italic>FATCAT</italic> (Ye & Godzik, 2003<xref ref-type="bibr" rid="bb63"> ▶</xref>).</p></sec></sec><sec sec-type="discussion|interpretation" id="sec3"><label>3.</label><title>Results and discussion</title><sec id="sec3.1"><label>3.1.</label><title>Overall structure</title><p>Residues 1–22 of the full-length protein (1–154) were initially predicted to represent a signal peptide and were removed during cloning. The crystallized protein is comprised of a glycine left after cleavage of the expression and purification tag followed by KPN03535 residues 23–154. The final model contains ten monomers (chains <italic>A</italic>–<italic>J</italic>), two PEG molecules (PEG 600 fragments from the crystallization solution) and 323 water molecules in the asymmetric unit. The ten monomers are almost identical in structure and completeness and superimpose extremely well, with pairwise r.m.s.d. values ranging from only 0.2 to 0.4 Å. Residues 23–35 in chains <italic>A</italic>
<italic>B</italic>, <italic>C</italic>, <italic>E</italic> and <italic>J</italic>, 23–36 and 154 in chain <italic>D</italic>, 23–35 and 154 in chain <italic>F</italic>, 23–36 in chains <italic>G</italic> and <italic>H</italic>, and 23–38 in chain <italic>I</italic> and the N-terminal glycine in all chains are disordered and have not been modeled. The Matthews coefficient (Matthews, 1968<xref ref-type="bibr" rid="bb37"> ▶</xref>) is ∼3.2 Å<sup>3</sup> Da<sup>−1</sup>, with an estimated solvent content of ∼62%. The Ramachandran plot produced by <italic>MolProbity</italic> (Davis <italic>et al.</italic>, 2004<xref ref-type="bibr" rid="bb9"> ▶</xref>) shows that 98.5% and 100% of amino acids are in the favored and allowed regions, respectively.</p><p>Residues 70–154 of the monomer form the OB-fold comprised of a five-stranded β-sheet (β1, β2, β3, β4 and β5) capped by a short α-helix (α) based on the standard OB-fold nomenclature (Murzin, 1993<xref ref-type="bibr" rid="bb40"> ▶</xref>; Fig. 1<xref ref-type="fig" rid="fig1"> ▶</xref><italic>a</italic>). The capping helix is shorter than those observed in most other OB-fold proteins (Fig. 2<xref ref-type="fig" rid="fig2"> ▶</xref>). Residues 36–69 constitute three additional α-helices (α−2, α−1 and α0) which are not observed in other structures of the same fold. The curved β-sheet forming the β-barrel core of the OB-fold is highly conserved in size and structure, while the largest variations are seen in the three loops (L<sub>12</sub>, L<sub>23</sub> and L<sub>45</sub>) that extend in different directions from the core and are often functionally important.</p><p>Crystal-packing and assembly analysis using <italic>PISA</italic> (Krissinel & Henrick, 2005<xref ref-type="bibr" rid="bb28"> ▶</xref>) supported by analytical size-exclusion chromatography and static light scattering suggest that a monomer is the likely oligomeric state. In the crystal structure, the protein assembles as two stacked pentameric rings, formed by loose interdigitation of the ‘finger-like’ β1–L<sub>12</sub>–β2 structure, with outer and inner diameters of ∼80 Å and ∼40 Å, respectively, and a thickness of ∼40 Å. The buried surface area of each monomer within each pentamer (∼540 Å<sup>2</sup>) and each monomer in the interface between the two pentamers (∼600 Å<sup>2</sup>) is low. The quaternary structure analysis does not suggest sufficiently strong and extensive interactions to enable complex formation in solution, suggesting that these pentamers could be a crystallization artifact. The N-terminus of each monomer extends into the solvent and probably does not have an impact on the oligomerization state. In the absence of any biochemical data, the functional oligomeric state of the protein remains unknown.</p></sec><sec id="sec3.2"><label>3.2.</label><title>Functional hypotheses</title><sec id="sec3.2.1"><label>3.2.1.</label><title>NlpE-like</title><p>The only other reported bacterial lipoprotein containing an OB-fold is the C-terminal domain of <italic>E. coli</italic> NlpE (new lipoprotein E), which is an outer membrane lipoprotein in Gram-negative bacteria involved in the envelope stress response in the Cpx pathway. It activates the Cpx, two-component, signal transduction pathway composed of the inner membrane histidine kinase CpxA and the cytoplasmic response regulator CpxR (Raivio & Silhavy, 1997<xref ref-type="bibr" rid="bb46"> ▶</xref>). The Cpx pathway controls the production of the periplasmic protease DegP and other proteins involved in fighting cellular stress (Snyder <italic>et al.</italic>, 1995<xref ref-type="bibr" rid="bb49"> ▶</xref>; Danese <italic>et al.</italic>, 1995<xref ref-type="bibr" rid="bb7"> ▶</xref>; Raivio <italic>et al.</italic>, 1999<xref ref-type="bibr" rid="bb45"> ▶</xref>). Other proteins are also implicated in the regulation of the Cpx pathway. For example, CpxP with an LT<italic>XX</italic>Q motif (Pfam PF07813) is involved in feedback inhibition of the Cpx pathway (Danese <italic>et al.</italic>, 1998<xref ref-type="bibr" rid="bb5"> ▶</xref>; Danese & Silhavy, 1998<xref ref-type="bibr" rid="bb6"> ▶</xref>). In <italic>K. pneumoniae</italic>, a periplasmic CpxP-like protein with the LT<italic>XX</italic>Q motif, KPN03534, is the neighboring gene to KPN03535. Therefore, KPN03535, like KPN03534, may play a role in the Cpx pathway, similar to NlpE. KPN03535 superimposes fairly well on <italic>E. coli</italic> NlpE (PDB code <ext-link ext-link-type="uri" xlink:href="http://scripts.iucr.org/cgi-bin/cr.cgi?rm=pdb&pdbId=2z4i">2z4i</ext-link>; Hirano <italic>et al.</italic>, 2007<xref ref-type="bibr" rid="bb20"> ▶</xref>; r.m.s.d. = 3.3 Å, 16% sequence identity, <italic>Z</italic> score 2.3; Fig. 2<xref ref-type="fig" rid="fig2"> ▶</xref><italic>a</italic>). Despite extremely low sequence identity, some residues are conserved in KPN03535 (Arg76, Asp100, Thr105, Lys107, Arg108 and Asn117) from structure-based sequence alignment. However, the functional roles of these residues in NlpE are not known.</p></sec><sec id="sec3.2.2"><label>3.2.2.</label><title>Toxin and BOF-like</title><p>Other bacterial OB-fold proteins that have an N-terminal signal sequence are toxins, such as the shiga toxin (PDB code <ext-link ext-link-type="uri" xlink:href="http://scripts.iucr.org/cgi-bin/cr.cgi?rm=pdb&pdbId=1r4p">1r4p</ext-link>; Fraser <italic>et al.</italic>, 2004<xref ref-type="bibr" rid="bb14"> ▶</xref>; Fig. 2<xref ref-type="fig" rid="fig2"> ▶</xref><italic>b</italic>), cholera toxin (PDB code <ext-link ext-link-type="uri" xlink:href="http://scripts.iucr.org/cgi-bin/cr.cgi?rm=pdb&pdbId=3efx">3efx</ext-link>; Holmner <italic>et al.</italic>, 2004<xref ref-type="bibr" rid="bb22"> ▶</xref>; r.m.s.d. = 2.8 Å, 6% sequence identity, <italic>Z</italic> score 5.8) and a bacterial OB-fold (BOF; Ginalski <italic>et al.</italic>, 2004<xref ref-type="bibr" rid="bb17"> ▶</xref>) protein (<ext-link ext-link-type="uri" xlink:href="http://scripts.iucr.org/cgi-bin/cr.cgi?rm=pdb&pdbId=1nnx">1nnx</ext-link>; O. Lehmann, A. Galkin, S. Pullalarevu, E. Sarikaya, W. Krajewski, K. Lim, A. Howard & O. Herzberg, unpublished work; r.m.s.d. = 2.9 Å, 14% sequence identity; <italic>Z</italic> score 7.4; Fig. 2<xref ref-type="fig" rid="fig2"> ▶</xref><italic>c</italic>). Neither NlpE nor the toxins have all three of the N-terminal helices (α0, α−1, α−2) found in KPN03535, but α−2 is observed in cholera toxin (<ext-link ext-link-type="uri" xlink:href="http://scripts.iucr.org/cgi-bin/cr.cgi?rm=pdb&pdbId=3efx">3efx</ext-link>) and α−1 is observed in BOF protein (<ext-link ext-link-type="uri" xlink:href="http://scripts.iucr.org/cgi-bin/cr.cgi?rm=pdb&pdbId=1nnx">1nnx</ext-link>). The capping helix α in KPN03535 is shorter than in the toxins and NlpE, although it is similar to that observed in BOF protein. The β-strands forming the curved β-barrel in all these structures are of similar length, but with differences in the loop sizes that connect the β-strands.</p></sec><sec id="sec3.2.3"><label>3.2.3.</label><title>Single-stranded DNA-binding protein, SSB-like</title><p>Single-stranded DNA-binding proteins (SSBs) also possess OB-folds and are involved in a multitude of cellular functions, such as DNA replication, transcription, recombination, repair, translation, cold-shock response and maintenance of telomeres (Theobald <italic>et al.</italic>, 2003<xref ref-type="bibr" rid="bb53"> ▶</xref>; Chase & Williams, 1986<xref ref-type="bibr" rid="bb2"> ▶</xref>; Wold, 1997<xref ref-type="bibr" rid="bb60"> ▶</xref>; Meyer & Laine, 1990<xref ref-type="bibr" rid="bb39"> ▶</xref>; Lohman & Ferrari, 1994<xref ref-type="bibr" rid="bb35"> ▶</xref>; Lohman <italic>et al.</italic>, 1996<xref ref-type="bibr" rid="bb36"> ▶</xref>). KPN03535 is structurally similar to OB-fold SSBs, including <italic>E. coli</italic> SSB (PDB code <ext-link ext-link-type="uri" xlink:href="http://scripts.iucr.org/cgi-bin/cr.cgi?rm=pdb&pdbId=1eyg">1eyg</ext-link>; Raghunathan <italic>et al.</italic>, 2000<xref ref-type="bibr" rid="bb44"> ▶</xref>; r.m.s.d. 2.7 Å; 13% sequence identity; <italic>Z</italic> score 7.0; Fig. 2<xref ref-type="fig" rid="fig2"> ▶</xref><italic>d</italic>), <italic>E. coli</italic> PriB (PDB code <ext-link ext-link-type="uri" xlink:href="http://scripts.iucr.org/cgi-bin/cr.cgi?rm=pdb&pdbId=1v1q">1v1q</ext-link>; Liu <italic>et al.</italic>, 2004<xref ref-type="bibr" rid="bb34"> ▶</xref>; r.m.s.d. 2.3 Å; 13% sequence identity, <italic>Z</italic> score 8.0; Fig. 2<xref ref-type="fig" rid="fig2"> ▶</xref><italic>e</italic>), <italic>Thermus thermophilus</italic> aspartyl-tRNA synthetase (PDB code <ext-link ext-link-type="uri" xlink:href="http://scripts.iucr.org/cgi-bin/cr.cgi?rm=pdb&pdbId=1l0w">1l0w</ext-link>; Ng <italic>et al.</italic>, 2002<xref ref-type="bibr" rid="bb42"> ▶</xref>; r.m.s.d. 2.6 Å; 11% sequence identity; <italic>Z</italic> score 9.0; Fig. 2<xref ref-type="fig" rid="fig2"> ▶</xref><italic>f</italic>) and human mitochondrial SSB (PDB code <ext-link ext-link-type="uri" xlink:href="http://scripts.iucr.org/cgi-bin/cr.cgi?rm=pdb&pdbId=3ull">3ull</ext-link>; Yang <italic>et al.</italic>, 1997<xref ref-type="bibr" rid="bb61"> ▶</xref>; r.m.s.d. 2.7 Å; 8% sequence identity, <italic>Z</italic> score 7.1). The N-terminal α−1 and α0 secondary-structure elements in KPN03535 are partially conserved in aspartyl-tRNA synthetase, but not in the other structures. Many of the loops in OB-fold ssDNA-binding proteins are either involved in interactions with DNA or in quaternary interactions that result in the various oligomeric forms. For example, loop L<sub>45</sub>, which makes the most interactions with DNA in PriB (Huang <italic>et al.</italic>, 2006<xref ref-type="bibr" rid="bb23"> ▶</xref>) and aspartyl-tRNA synthetase, is similar to that of KPN03535, but is much longer in <italic>E. coli</italic> and in human mitochondrial SSBs. Among the surface-exposed Arg, Lys and aromatic residues that could be functionally relevant if KPN03535 were to bind DNA or RNA (Fig. 3<xref ref-type="fig" rid="fig3"> ▶</xref>), Arg84 and Lys85 of KPN03535 are conserved and correspond to Arg17 and Lys18 in PriB, where Lys18 is involved in ssDNA-binding (Huang <italic>et al.</italic>, 2006<xref ref-type="bibr" rid="bb23"> ▶</xref>). Arg83 and Arg99 of KPN03535 are conserved in aspartyl tRNA synthetase as Arg29 (equivalent to Arg28 in the <italic>E. coli</italic> aspartyl-tRNA synthetase that binds to tRNA; Eiler <italic>et al.</italic>, 1999<xref ref-type="bibr" rid="bb11"> ▶</xref>) and Arg39. Multiple structural alignment of various OB-fold proteins using the <italic>POSA</italic> method (Ye & Godzik, 2005<xref ref-type="bibr" rid="bb64"> ▶</xref>) suggests that KPN03535 has a closer relationship to tRNA synthetases than to the BOF protein and is most distant from OB-fold toxins.</p><p>Analysis of the electrostatic surface potential indicates that KPN03535 most closely resembles PriB and aspartyl-tRNA synthetase (Fig. 4<xref ref-type="fig" rid="fig4"> ▶</xref>), with a prominent positively charged area similar to the DNA-binding region of these two proteins. Interestingly, this patch is different from that observed in the <italic>E. coli</italic> SSB, which reflects the known differences in ssDNA-binding modes of SSB and PriB. The basic nature of KPN03535 (pI 9.4) also hints at the possibility of oligonucleotide binding.</p><p>In conclusion, the crystal structure of KPN03535 reveals a novel divergent member of the prevalent OB-fold and suggests that it is most likely to be a nucleic acid-binding protein. As for the recently solved structure of MPN554 from <italic>Mycoplasma pneumoniae</italic> (Das <italic>et al.</italic>, 2007<xref ref-type="bibr" rid="bb8"> ▶</xref>), another novel OB-fold with unknown cellular function but with single-stranded DNA-binding properties, the structure of KPN03535 reveals that further exploration of the functionality of the OB-fold is necessary. Bacterial lipoproteins have many important functions and are potential vaccine candidates (Steere <italic>et al.</italic>, 1998<xref ref-type="bibr" rid="bb50"> ▶</xref>; Myers <italic>et al.</italic>, 2007<xref ref-type="bibr" rid="bb41"> ▶</xref>). <italic>K. pneumoniae</italic> is an opportunistic pathogen that is prevalent in immunocompromised patients in hospitals and in patients with liver disease (Hidron <italic>et al.</italic>, 2008<xref ref-type="bibr" rid="bb19"> ▶</xref>; Pope <italic>et al.</italic>, 2008<xref ref-type="bibr" rid="bb43"> ▶</xref>). Functional inferences that can be drawn from this crystal structure should now allow focused structure-assisted biochemistry to establish the exact molecular and cellular role for this protein.</p><p>Additional information about KPN03535 is available from TOPSAN (Krishna <italic>et al.</italic>, 2010<xref ref-type="bibr" rid="bb67"> ▶</xref>) <ext-link ext-link-type="uri" xlink:href="http://www.topsan.org/explore?PDBid=3f1z">http://www.topsan.org/explore?PDBid=3f1z</ext-link>.</p></sec></sec></sec><sec sec-type="supplementary-material"><title>Supplementary Material</title><supplementary-material position="float" xlink:type="simple"><p>PDB reference: <ext-link ext-link-type="pdb" xlink:href="3flz" xlink:type="simple">KPN03535, 3flz, r3f1zsf</ext-link></p></supplementary-material></sec></body><back><ack><p>This work was supported by the National Institute of General Medical Sciences, Protein Structure Initiative Grant <award-id>U54</award-id> GM074898. Portions of this research were performed at the Stanford Synchrotron Radiation Lightsource (SSRL). SSRL is a national user facility at SLAC National Accelerator Laboratory, operated by Stanford University on behalf of the United States Department of Energy, Office of Basic Energy Sciences. The SSRL Structural Molecular Biology Program is supported by the Department of Energy, Office of Biological and Environmental Research and by the <funding-source>National Institutes of Health</funding-source> (National Center for Research Resources, Biomedical Technology Program and the National Institute of General Medical Sciences). The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institute of General Medical Sciences or the National Institutes of Health. 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(<italic>a</italic>) Stereo ribbon representation of the KPN03535 monomer color-coded from the N-terminus (yellow) to the C-terminus (green). The nomenclature for helix α and strands β1–β5 follows that used for the OB-fold (Murzin, 1993<xref ref-type="bibr" rid="bb40"> ▶</xref>). Helices α−2, α−1 and α0 are unique to KPN03535. (<italic>b</italic>) Diagram showing the secondary-structure elements of KPN03535 superimposed on the primary amino-acid sequence. Helices and β-strands are indicated. The protein was expressed with a purification tag that was removed, leaving a residual Gly residue at the N-terminus followed by the KPN03535 sequence.</p></caption><graphic xlink:href="f-66-01254-fig1"></graphic></fig><fig id="fig2" position="float"><label>Figure 2</label><caption><p>Superimposition of the crystal structure of KPN03535 (red) on OB-fold proteins that have N-terminal lipoprotein sequence, such as (<italic>a</italic>) NlpE, (<italic>b</italic>) shiga toxin and (<italic>c</italic>) BOF, and single-stranded DNA-binding proteins (SSBs), such as (<italic>d</italic>) <italic>E. coli</italic> SSB, (<italic>e</italic>) <italic>E. coli</italic> PriB and (<italic>f</italic>) <italic>T. thermophilus</italic> aspartyl-tRNA synthetase.</p></caption><graphic xlink:href="f-66-01254-fig2"></graphic></fig><fig id="fig3" position="float"><label>Figure 3</label><caption><p>Surface-exposed charged and aromatic residues on KPN03535 that may be functionally important if this protein binds DNA or RNA (for clarity, the view of the monomer shown here is different from that shown in Fig. 4<xref ref-type="fig" rid="fig4"> ▶</xref> and was obtained by a 180° rotation around a horizontal axis followed by a 180° rotation around a vertical axis). Arg83, Arg84 and Lys85 comprise the positive surface region described in Fig. 4<xref ref-type="fig" rid="fig4"> ▶</xref>. Arg84 and Lys85 are conserved as Arg17 and Lys18 in the <italic>E. coli</italic> PriB structure and as Arg29 in <italic>T. thermophilus</italic> aspartyl-tRNA synthetase. Phe94 is conserved in shiga toxin, but there are currently no reports of any functional role of this residue in the toxin.</p></caption><graphic xlink:href="f-66-01254-fig3"></graphic></fig><fig id="fig4" position="float"><label>Figure 4</label><caption><p>Comparison of the electrostatic surface potentials of monomers of (<italic>a</italic>) NlpE, (<italic>b</italic>) shiga toxin, (<italic>c</italic>) BOF, (<italic>d</italic>) <italic>E. coli</italic> SSB, (<italic>e</italic>) <italic>E. coli</italic> PriB, (<italic>f</italic>) <italic>T. thermophilus</italic> aspartyl-tRNA synthetase and (<italic>g</italic>) KPN03535. All the figures are in approximately the same orientation and reflect the surface view that would be presented for oligonucleotide binding, as in tRNA synthetase. The figure reveals that the positively charged surface patch (central blue portion in black circles) on the KPN03535 most closely resembles that of <italic>E. coli</italic> PriB and is also similar to that seen in aspartyl-tRNA synthetase. In KPN03535, this positively charged patch is formed by Arg83, Arg84 and Lys85. The corresponding conserved residues are Arg17 and Lys18 in PriB and Arg29 in aspartyl-tRNA synthetases, respectively.</p></caption><graphic xlink:href="f-66-01254-fig4"></graphic></fig><table-wrap id="table1" position="float"><label>Table 1</label><caption><title>Crystallographic data and refinement statistics for KPN03535 (PDB code <ext-link ext-link-type="uri" xlink:href="http://scripts.iucr.org/cgi-bin/cr.cgi?rm=pdb&pdbId=3f1z">3f1z</ext-link>)</title><p>Values in parentheses are for the highest resolution shell.</p></caption><table frame="hsides" rules="groups"><tbody valign="top"><tr><td style="" rowspan="1" colspan="1" align="left" valign="top">Space group</td><td style="" rowspan="1" colspan="1" align="left" valign="top"><italic>P</italic>2<sub>1</sub>2<sub>1</sub>2<sub>1</sub></td></tr><tr><td style="" rowspan="1" colspan="1" align="left" valign="top">Unit-cell parameters (Å)</td><td style="" rowspan="1" colspan="1" align="left" valign="top"><italic>a</italic> = 97.42, <italic>b</italic> = 105.51, <italic>c</italic> = 181.25</td></tr><tr><td style="" rowspan="1" colspan="1" align="left" valign="top">Data collection</td><td style="" rowspan="1" colspan="1" align="left" valign="top"> </td></tr><tr><td style="" rowspan="1" colspan="1" align="left" valign="top"> Wavelength (Å)</td><td style="" rowspan="1" colspan="1" align="left" valign="top">0.9792 [Se peak (λ<sub>1</sub>)]</td></tr><tr><td style="" rowspan="1" colspan="1" align="left" valign="top"> Resolution range (Å)</td><td style="" rowspan="1" colspan="1" align="left" valign="top">29.9–2.46 (2.52–2.46)</td></tr><tr><td style="" rowspan="1" colspan="1" align="left" valign="top"> No. of observations</td><td style="" rowspan="1" colspan="1" align="left" valign="top">509996</td></tr><tr><td style="" rowspan="1" colspan="1" align="left" valign="top"> No. of unique reflections</td><td style="" rowspan="1" colspan="1" align="left" valign="top">68362</td></tr><tr><td style="" rowspan="1" colspan="1" align="left" valign="top"> Completeness (%)</td><td style="" rowspan="1" colspan="1" align="left" valign="top">99.8 (99.7)</td></tr><tr><td style="" rowspan="1" colspan="1" align="left" valign="top"> Mean <italic>I</italic>/σ(<italic>I</italic>)</td><td style="" rowspan="1" colspan="1" align="left" valign="top">15.4 (2.5)</td></tr><tr><td style="" rowspan="1" colspan="1" align="left" valign="top">
<italic>R</italic><sub>merge</sub> on <italic>I</italic><xref ref-type="table-fn" rid="tfn1">†</xref> (%)</td><td style="" rowspan="1" colspan="1" align="left" valign="top">11.1 (69.6)</td></tr><tr><td style="" rowspan="1" colspan="1" align="left" valign="top">Model and refinement statistics</td><td style="" rowspan="1" colspan="1" align="left" valign="top"> </td></tr><tr><td style="" rowspan="1" colspan="1" align="left" valign="top"> Resolution range (Å)</td><td style="" rowspan="1" colspan="1" align="left" valign="top">29.9–2.46</td></tr><tr><td style="" rowspan="1" colspan="1" align="left" valign="top"> No. of reflections (total)</td><td style="" rowspan="1" colspan="1" align="left" valign="top">68310<xref ref-type="table-fn" rid="tfn2">‡</xref></td></tr><tr><td style="" rowspan="1" colspan="1" align="left" valign="top"> No. of reflections (test)</td><td style="" rowspan="1" colspan="1" align="left" valign="top">3458</td></tr><tr><td style="" rowspan="1" colspan="1" align="left" valign="top"> Completeness (%)</td><td style="" rowspan="1" colspan="1" align="left" valign="top">99.7</td></tr><tr><td style="" rowspan="1" colspan="1" align="left" valign="top"> Data set used in refinement</td><td style="" rowspan="1" colspan="1" align="left" valign="top">λ<sub>1</sub></td></tr><tr><td style="" rowspan="1" colspan="1" align="left" valign="top"> Cutoff criterion</td><td style="" rowspan="1" colspan="1" align="left" valign="top">|<italic>F</italic>| > 0</td></tr><tr><td style="" rowspan="1" colspan="1" align="left" valign="top">
<italic>R</italic><sub>cryst</sub><xref ref-type="table-fn" rid="tfn3">§</xref></td><td style="" rowspan="1" colspan="1" align="left" valign="top">0.192</td></tr><tr><td style="" rowspan="1" colspan="1" align="left" valign="top">
<italic>R</italic><sub>free</sub><xref ref-type="table-fn" rid="tfn3">§</xref></td><td style="" rowspan="1" colspan="1" align="left" valign="top">0.228</td></tr><tr><td style="" rowspan="1" colspan="1" align="left" valign="top">Stereochemical parameters</td><td style="" rowspan="1" colspan="1" align="left" valign="top"> </td></tr><tr><td style="" rowspan="1" colspan="1" align="left" valign="top"> Restraints (r.m.s.d. observed)</td><td style="" rowspan="1" colspan="1" align="left" valign="top"> </td></tr><tr><td style="" rowspan="1" colspan="1" align="left" valign="top"> Bond angle (°)</td><td style="" rowspan="1" colspan="1" align="left" valign="top">1.70</td></tr><tr><td style="" rowspan="1" colspan="1" align="left" valign="top"> Bond length (Å)</td><td style="" rowspan="1" colspan="1" align="left" valign="top">0.017</td></tr><tr><td style="" rowspan="1" colspan="1" align="left" valign="top"> Average isotropic <italic>B</italic> value (Å<sup>2</sup>)</td><td style="" rowspan="1" colspan="1" align="left" valign="top">38.2<xref ref-type="table-fn" rid="tfn4">¶</xref></td></tr><tr><td style="" rowspan="1" colspan="1" align="left" valign="top"> ESU<xref ref-type="table-fn" rid="tfn5">††</xref> based on <italic>R</italic><sub>free</sub> (Å)</td><td style="" rowspan="1" colspan="1" align="left" valign="top">0.22</td></tr><tr><td style="" rowspan="1" colspan="1" align="left" valign="top"> Protein residues/atoms</td><td style="" rowspan="1" colspan="1" align="left" valign="top">1182/9162</td></tr><tr><td style="" rowspan="1" colspan="1" align="left" valign="top"> Water/PEG molecules</td><td style="" rowspan="1" colspan="1" align="left" valign="top">323/2</td></tr></tbody></table><table-wrap-foot><fn id="tfn1"><label>†</label><p><italic>R</italic><sub>merge</sub> = <inline-formula><inline-graphic xlink:href="f-66-01254-efi1.jpg" mimetype="image" mime-subtype="gif"></inline-graphic></inline-formula><inline-formula><inline-graphic xlink:href="f-66-01254-efi2.jpg" mimetype="image" mime-subtype="gif"></inline-graphic></inline-formula>.</p></fn><fn id="tfn2"><label>‡</label><p>Typically, the number of unique reflections used in refinement is slightly less than the total number that were integrated and scaled. Reflections are excluded owing to systematic absences, negative intensities and rounding errors in the resolution limits and unit-cell parameters.</p></fn><fn id="tfn3"><label>§</label><p><italic>R</italic><sub>cryst</sub> = <inline-formula><inline-graphic xlink:href="f-66-01254-efi3.jpg" mimetype="image" mime-subtype="gif"></inline-graphic></inline-formula><inline-formula><inline-graphic xlink:href="f-66-01254-efi4.jpg" mimetype="image" mime-subtype="gif"></inline-graphic></inline-formula>, where <italic>F</italic><sub>calc</sub> and <italic>F</italic><sub>obs</sub> are the calculated and observed structure-factor amplitudes, respectively. <italic>R</italic><sub>free</sub> is as for <italic>R</italic><sub>cryst</sub>, but for 5.1% of the total reflections chosen at random and omitted from refinement.</p></fn><fn id="tfn4"><label>¶</label><p>This value represents the total <italic>B</italic> that includes TLS and residual <italic>B</italic> components.</p></fn><fn id="tfn5"><label>††</label><p>ESU, estimated overall coordinate error (Collaborative Computational Project, Number 4, 1994<xref ref-type="bibr" rid="bb4"> ▶</xref>; Tickle <italic>et al.</italic>, 1998<xref ref-type="bibr" rid="bb55"> ▶</xref>).</p></fn></table-wrap-foot></table-wrap></floats-group></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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