The High-Precision Solution Structure of Yersinia Modulating Protein YmoA Provides Insight into Interaction with H-NS†
Identifieur interne : 002B82 ( Main/Exploration ); précédent : 002B81; suivant : 002B83The High-Precision Solution Structure of Yersinia Modulating Protein YmoA Provides Insight into Interaction with H-NS†
Auteurs : Robert L. Mcfeeters [États-Unis] ; Amanda S. Altieri [États-Unis] ; Scott Cherry [États-Unis] ; Joseph E. Tropea [États-Unis] ; David S. Waugh [États-Unis] ; R. Andrew Byrd [États-Unis]Source :
- Biochemistry [ 0006-2960 ] ; 2007.
Abstract
The high-resolution solution structure of Yersinia modulating protein YmoA is presented. The protein is all helical with the first three of four helices forming the central core. Structures calculated with only NOE and dihedral restraints exhibit a backbone root-mean-square deviation (rmsd) of 0.77 Å. Upon refinement against Hα−Cα, HN−N, and Cα−C‘ J-modulated residual dipolar couplings, the backbone rmsd improves to 0.22 Å. YmoA has a high amino acid sequence identity to and a similar overall fold to Escherichia coli hemolysin expression modulating protein Hha; however, structural differences do occur. YmoA is also found to be structurally similar to the histone-like nucleoid structuring protein H-NS, indicating that YmoA may intercalate into higher-order H-NS suprastructuring by substituting for an H-NS dimer.
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DOI: 10.1021/bi701210j
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Tropea</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Maryland</region></placeName><wicri:cityArea>Structural Biophysics Laboratory and Macromolecular Crystallography Laboratory, Center for Cancer Research, NationalCancer Institute, Frederick</wicri:cityArea></affiliation><affiliation></affiliation></author><author><name sortKey="Waugh, David S" sort="Waugh, David S" uniqKey="Waugh D" first="David S." last="Waugh">David S. Waugh</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Maryland</region></placeName><wicri:cityArea>Structural Biophysics Laboratory and Macromolecular Crystallography Laboratory, Center for Cancer Research, NationalCancer Institute, Frederick</wicri:cityArea></affiliation><affiliation></affiliation></author><author><name sortKey="Byrd, R Andrew" sort="Byrd, R Andrew" uniqKey="Byrd R" first="R. Andrew" last="Byrd">R. Andrew Byrd</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Maryland</region></placeName><wicri:cityArea>Structural Biophysics Laboratory and Macromolecular Crystallography Laboratory, Center for Cancer Research, NationalCancer Institute, Frederick</wicri:cityArea></affiliation><affiliation></affiliation><affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j" type="main">Biochemistry</title><title level="j" type="abbrev">Biochemistry</title><idno type="ISSN">0006-2960</idno><idno type="eISSN">1520-4995</idno><imprint><publisher>American Chemical Society</publisher><date type="e-published">2007</date><date type="published">2007</date><biblScope unit="vol">46</biblScope><biblScope unit="issue">49</biblScope><biblScope unit="page" from="13975">13975</biblScope><biblScope unit="page" to="13982">13982</biblScope></imprint><idno type="ISSN">0006-2960</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0006-2960</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract">The high-resolution solution structure of Yersinia modulating protein YmoA is presented. The protein is all helical with the first three of four helices forming the central core. Structures calculated with only NOE and dihedral restraints exhibit a backbone root-mean-square deviation (rmsd) of 0.77 Å. Upon refinement against Hα−Cα, HN−N, and Cα−C‘ J-modulated residual dipolar couplings, the backbone rmsd improves to 0.22 Å. YmoA has a high amino acid sequence identity to and a similar overall fold to Escherichia coli hemolysin expression modulating protein Hha; however, structural differences do occur. YmoA is also found to be structurally similar to the histone-like nucleoid structuring protein H-NS, indicating that YmoA may intercalate into higher-order H-NS suprastructuring by substituting for an H-NS dimer.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Maryland</li></region></list><tree><country name="États-Unis"><region name="Maryland"><name sortKey="Mcfeeters, Robert L" sort="Mcfeeters, Robert L" uniqKey="Mcfeeters R" first="Robert L." last="Mcfeeters">Robert L. Mcfeeters</name></region><name sortKey="Altieri, Amanda S" sort="Altieri, Amanda S" uniqKey="Altieri A" first="Amanda S." last="Altieri">Amanda S. Altieri</name><name sortKey="Byrd, R Andrew" sort="Byrd, R Andrew" uniqKey="Byrd R" first="R. Andrew" last="Byrd">R. Andrew Byrd</name><name sortKey="Cherry, Scott" sort="Cherry, Scott" uniqKey="Cherry S" first="Scott" last="Cherry">Scott Cherry</name><name sortKey="Tropea, Joseph E" sort="Tropea, Joseph E" uniqKey="Tropea J" first="Joseph E." last="Tropea">Joseph E. Tropea</name><name sortKey="Waugh, David S" sort="Waugh, David S" uniqKey="Waugh D" first="David S." last="Waugh">David S. Waugh</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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