Links to Exploration step
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Proteolytic activation of <italic>Chlamydia trachomatis</italic> HTRA is mediated by PDZ1 domain interactions with protease domain loops L3 and LC and beta strand β5</title><author><name sortKey="Marsh, James W" sort="Marsh, James W" uniqKey="Marsh J" first="James W." last="Marsh">James W. Marsh</name><affiliation><nlm:aff id="Aff1"><institution-wrap><institution-id institution-id-type="GRID">grid.1024.7</institution-id><institution-id institution-id-type="ISNI">0000000089150953</institution-id><institution>Institute of Health and Biomedical Innovation (IHBI),</institution><institution>Queensland University of Technology (QUT),</institution></institution-wrap>60 Musk Avenue, Kelvin Grove, Queensland Australia 4059</nlm:aff></affiliation></author><author><name sortKey="Lott, William B" sort="Lott, William B" uniqKey="Lott W" first="William B." last="Lott">William B. Lott</name><affiliation><nlm:aff id="Aff1"><institution-wrap><institution-id institution-id-type="GRID">grid.1024.7</institution-id><institution-id institution-id-type="ISNI">0000000089150953</institution-id><institution>Institute of Health and Biomedical Innovation (IHBI),</institution><institution>Queensland University of Technology (QUT),</institution></institution-wrap>60 Musk Avenue, Kelvin Grove, Queensland Australia 4059</nlm:aff></affiliation></author><author><name sortKey="Tyndall, Joel D A" sort="Tyndall, Joel D A" uniqKey="Tyndall J" first="Joel D. A." last="Tyndall">Joel D. A. Tyndall</name><affiliation><nlm:aff id="Aff2"><institution-wrap><institution-id institution-id-type="GRID">grid.29980.3a</institution-id><institution-id institution-id-type="ISNI">0000000419367830</institution-id><institution>National School of Pharmacy,</institution><institution>University of Otago,</institution></institution-wrap>PO Box 56, Dunedin, New Zealand 9054</nlm:aff></affiliation></author><author><name sortKey="Huston, Wilhelmina Willa M" sort="Huston, Wilhelmina Willa M" uniqKey="Huston W" first="Wilhelmina Willa M." last="Huston">Wilhelmina Willa M. Huston</name><affiliation><nlm:aff id="Aff1"><institution-wrap><institution-id institution-id-type="GRID">grid.1024.7</institution-id><institution-id institution-id-type="ISNI">0000000089150953</institution-id><institution>Institute of Health and Biomedical Innovation (IHBI),</institution><institution>Queensland University of Technology (QUT),</institution></institution-wrap>60 Musk Avenue, Kelvin Grove, Queensland Australia 4059</nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">24036669</idno><idno type="pmc">6275972</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6275972</idno><idno type="RBID">PMC:6275972</idno><idno type="doi">10.2478/s11658-013-0103-2</idno><date when="2013">2013</date><idno type="wicri:Area/Pmc/Corpus">000347</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000347</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Proteolytic activation of <italic>Chlamydia trachomatis</italic> HTRA is mediated by PDZ1 domain interactions with protease domain loops L3 and LC and beta strand β5</title><author><name sortKey="Marsh, James W" sort="Marsh, James W" uniqKey="Marsh J" first="James W." last="Marsh">James W. Marsh</name><affiliation><nlm:aff id="Aff1"><institution-wrap><institution-id institution-id-type="GRID">grid.1024.7</institution-id><institution-id institution-id-type="ISNI">0000000089150953</institution-id><institution>Institute of Health and Biomedical Innovation (IHBI),</institution><institution>Queensland University of Technology (QUT),</institution></institution-wrap>60 Musk Avenue, Kelvin Grove, Queensland Australia 4059</nlm:aff></affiliation></author><author><name sortKey="Lott, William B" sort="Lott, William B" uniqKey="Lott W" first="William B." last="Lott">William B. Lott</name><affiliation><nlm:aff id="Aff1"><institution-wrap><institution-id institution-id-type="GRID">grid.1024.7</institution-id><institution-id institution-id-type="ISNI">0000000089150953</institution-id><institution>Institute of Health and Biomedical Innovation (IHBI),</institution><institution>Queensland University of Technology (QUT),</institution></institution-wrap>60 Musk Avenue, Kelvin Grove, Queensland Australia 4059</nlm:aff></affiliation></author><author><name sortKey="Tyndall, Joel D A" sort="Tyndall, Joel D A" uniqKey="Tyndall J" first="Joel D. A." last="Tyndall">Joel D. A. Tyndall</name><affiliation><nlm:aff id="Aff2"><institution-wrap><institution-id institution-id-type="GRID">grid.29980.3a</institution-id><institution-id institution-id-type="ISNI">0000000419367830</institution-id><institution>National School of Pharmacy,</institution><institution>University of Otago,</institution></institution-wrap>PO Box 56, Dunedin, New Zealand 9054</nlm:aff></affiliation></author><author><name sortKey="Huston, Wilhelmina Willa M" sort="Huston, Wilhelmina Willa M" uniqKey="Huston W" first="Wilhelmina Willa M." last="Huston">Wilhelmina Willa M. Huston</name><affiliation><nlm:aff id="Aff1"><institution-wrap><institution-id institution-id-type="GRID">grid.1024.7</institution-id><institution-id institution-id-type="ISNI">0000000089150953</institution-id><institution>Institute of Health and Biomedical Innovation (IHBI),</institution><institution>Queensland University of Technology (QUT),</institution></institution-wrap>60 Musk Avenue, Kelvin Grove, Queensland Australia 4059</nlm:aff></affiliation></author></analytic><series><title level="j">Cellular & Molecular Biology Letters</title><idno type="ISSN">1425-8153</idno><idno type="eISSN">1689-1392</idno><imprint><date when="2013">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p><italic>Chlamydia trachomatis</italic> is a bacterial pathogen responsible for one of the most prevalent sexually transmitted infections worldwide. Its unique development cycle has limited our understanding of its pathogenic mechanisms. However, CtHtrA has recently been identified as a potential <italic>C. trachomatis</italic> virulence factor. CtHtrA is a tightly regulated quality control protein with a monomeric structural unit comprised of a chymotrypsin-like protease domain and two PDZ domains. Activation of proteolytic activity relies on the C-terminus of the substrate allosterically binding to the PDZ1 domain, which triggers subsequent conformational change and oligomerization of the protein into 24-mers enabling proteolysis. This activation is mediated by a cascade of precise structural arrangements, but the specific CtHtrA residues and structural elements required to facilitate activation are unknown. Using <italic>in vitro</italic> analysis guided by homology modeling, we show that the mutation of residues Arg362 and Arg224, predicted to disrupt the interaction between the CtHtrA PDZ1 domain and loop L3, and between loop L3 and loop LD, respectively, are critical for the activation of proteolytic activity. We also demonstrate that mutation to residues Arg299 and Lys160, predicted to disrupt PDZ1 domain interactions with protease loop LC and strand β5, are also able to influence proteolysis, implying their involvement in the CtHtrA mechanism of activation. This is the first investigation of protease loop LC and strand β5 with respect to their potential interactions with the PDZ1 domain. Given their high level of conservation in bacterial HtrA, these structural elements may be equally significant in the activation mechanism of DegP and other HtrA family members.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Stephens, Rs" uniqKey="Stephens R">RS Stephens</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Low, N" uniqKey="Low N">N Low</name></author></analytic></biblStruct><biblStruct></biblStruct><biblStruct><analytic><author><name sortKey="Pedersen, Ll" uniqKey="Pedersen L">LL Pedersen</name></author><author><name sortKey="Radulic, Mm" uniqKey="Radulic M">MM Radulic</name></author><author><name sortKey="Doric, Mm" uniqKey="Doric M">MM Doric</name></author><author><name sortKey="Kwaik, Yya" uniqKey="Kwaik Y">YYA Kwaik</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Lewis, C" uniqKey="Lewis C">C Lewis</name></author><author><name sortKey="Skovierova, H" uniqKey="Skovierova H">H Skovierova</name></author><author><name sortKey="Rowley, G" uniqKey="Rowley G">G Rowley</name></author><author><name sortKey="Rezuchova, B" uniqKey="Rezuchova B">B Rezuchova</name></author><author><name sortKey="Homerova, D" uniqKey="Homerova D">D Homerova</name></author><author><name sortKey="Stevenson, A" uniqKey="Stevenson A">A Stevenson</name></author><author><name sortKey="Spencer, J" uniqKey="Spencer J">J Spencer</name></author><author><name sortKey="Farn, J" uniqKey="Farn J">J Farn</name></author><author><name sortKey="Kormanec, J" uniqKey="Kormanec J">J Kormanec</name></author><author><name sortKey="Roberts, M" uniqKey="Roberts M">M Roberts</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Hoy, B" uniqKey="Hoy B">B Hoy</name></author><author><name sortKey="Lower, M" uniqKey="Lower M">M Lower</name></author><author><name sortKey="Weydig, C" uniqKey="Weydig C">C Weydig</name></author><author><name sortKey="Carra, G" uniqKey="Carra G">G Carra</name></author><author><name sortKey="Tegtmeyer, N" uniqKey="Tegtmeyer N">N Tegtmeyer</name></author><author><name sortKey="Geppert, T" uniqKey="Geppert T">T Geppert</name></author><author><name sortKey="Schroder, P" uniqKey="Schroder P">P Schroder</name></author><author><name sortKey="Sewald, N" uniqKey="Sewald N">N Sewald</name></author><author><name sortKey="Backert, S" uniqKey="Backert S">S Backert</name></author><author><name sortKey="Schneider, G" uniqKey="Schneider G">G Schneider</name></author><author><name sortKey="Wessler, S" uniqKey="Wessler S">S Wessler</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Strauch, Kl" uniqKey="Strauch K">KL Strauch</name></author><author><name sortKey="Beckwith, J" uniqKey="Beckwith J">J Beckwith</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Lipinska, Bb" uniqKey="Lipinska B">BB Lipinska</name></author><author><name sortKey="Zylicz, M" uniqKey="Zylicz M">M Zylicz</name></author><author><name sortKey="Georgopoulos, Cc" uniqKey="Georgopoulos C">CC Georgopoulos</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Spiess, Cc" uniqKey="Spiess C">CC Spiess</name></author><author><name sortKey="Beil, Aa" uniqKey="Beil A">AA Beil</name></author><author><name sortKey="Ehrmann, Mm" uniqKey="Ehrmann M">MM Ehrmann</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Baldi, A" uniqKey="Baldi A">A Baldi</name></author><author><name sortKey="De Luca, A" uniqKey="De Luca A">A De Luca</name></author><author><name sortKey="Morini, M" uniqKey="Morini M">M Morini</name></author><author><name sortKey="Battista, T" uniqKey="Battista T">T Battista</name></author><author><name sortKey="Felsani, A" uniqKey="Felsani A">A Felsani</name></author><author><name sortKey="Baldi, F" uniqKey="Baldi F">F Baldi</name></author><author><name sortKey="Catricala, C" uniqKey="Catricala C">C Catricalà</name></author><author><name sortKey="Amantea, A" uniqKey="Amantea A">A Amantea</name></author><author><name sortKey="Noonan, Dm" uniqKey="Noonan D">DM Noonan</name></author><author><name sortKey="Albini, A" uniqKey="Albini A">A Albini</name></author><author><name sortKey="Natali, Pg" uniqKey="Natali P">PG Natali</name></author><author><name sortKey="Lombardi, D" uniqKey="Lombardi D">D Lombardi</name></author><author><name sortKey="Paggi, Mg" uniqKey="Paggi M">MG Paggi</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Li, W" uniqKey="Li W">W Li</name></author><author><name sortKey="Srinivasula, Sm" uniqKey="Srinivasula S">SM Srinivasula</name></author><author><name sortKey="Chai, J" uniqKey="Chai J">J Chai</name></author><author><name sortKey="Li, P" uniqKey="Li P">P Li</name></author><author><name sortKey="Wu, J" uniqKey="Wu J">J Wu</name></author><author><name sortKey="Zhang, Z" uniqKey="Zhang Z">Z Zhang</name></author><author><name sortKey="Alnemri, Es" uniqKey="Alnemri E">ES Alnemri</name></author><author><name sortKey="Shi, Y" uniqKey="Shi Y">Y Shi</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Clausen, T" uniqKey="Clausen T">T Clausen</name></author><author><name sortKey="Southan, C" uniqKey="Southan C">C Southan</name></author><author><name sortKey="Ehrmann, Mm" uniqKey="Ehrmann M">MM Ehrmann</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Grau, S" uniqKey="Grau S">S Grau</name></author><author><name sortKey="Baldi, A" uniqKey="Baldi A">A Baldi</name></author><author><name sortKey="Bussani, R" uniqKey="Bussani R">R Bussani</name></author><author><name sortKey="Tian, X" uniqKey="Tian X">X Tian</name></author><author><name sortKey="Stefanescu, R" uniqKey="Stefanescu R">R Stefanescu</name></author><author><name sortKey="Przybylski, M" uniqKey="Przybylski M">M Przybylski</name></author><author><name sortKey="Richards, P" uniqKey="Richards P">P Richards</name></author><author><name sortKey="Jones, Sa" uniqKey="Jones S">SA Jones</name></author><author><name sortKey="Shridhar, V" uniqKey="Shridhar V">V Shridhar</name></author><author><name sortKey="Clausen, T" uniqKey="Clausen T">T Clausen</name></author><author><name sortKey="Ehrmann, Mm" uniqKey="Ehrmann M">MM Ehrmann</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Hansen, G" uniqKey="Hansen G">G Hansen</name></author><author><name sortKey="Hilgenfeld, R" uniqKey="Hilgenfeld R">R Hilgenfeld</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Rawlings, Nd" uniqKey="Rawlings N">ND Rawlings</name></author><author><name sortKey="Barrett, Aj" uniqKey="Barrett A">AJ Barrett</name></author><author><name sortKey="Bateman, A" uniqKey="Bateman A">A Bateman</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Spiers, A" uniqKey="Spiers A">A Spiers</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Kolmar, Hh" uniqKey="Kolmar H">HH Kolmar</name></author><author><name sortKey="Waller, Pr" uniqKey="Waller P">PR Waller</name></author><author><name sortKey="Sauer, Rt" uniqKey="Sauer R">RT Sauer</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Kim, Ss" uniqKey="Kim S">SS Kim</name></author><author><name sortKey="Sauer, Rt" uniqKey="Sauer R">RT Sauer</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Krojer, T" uniqKey="Krojer T">T Krojer</name></author><author><name sortKey="Garrido Franco, M" uniqKey="Garrido Franco M">M Garrido-Franco</name></author><author><name sortKey="Huber, R" uniqKey="Huber R">R Huber</name></author><author><name sortKey="Ehrmann, Mm" uniqKey="Ehrmann M">MM Ehrmann</name></author><author><name sortKey="Clausen, T" uniqKey="Clausen T">T Clausen</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Krojer, T" uniqKey="Krojer T">T Krojer</name></author><author><name sortKey="Sawa, J" uniqKey="Sawa J">J Sawa</name></author><author><name sortKey="Huber, R" uniqKey="Huber R">R Huber</name></author><author><name sortKey="Clausen, T" uniqKey="Clausen T">T Clausen</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Clausen, T" uniqKey="Clausen T">T Clausen</name></author><author><name sortKey="Kaiser, M" uniqKey="Kaiser M">M Kaiser</name></author><author><name sortKey="Huber, R" uniqKey="Huber R">R Huber</name></author><author><name sortKey="Ehrmann, Mm" uniqKey="Ehrmann M">MM Ehrmann</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Jiang, J" uniqKey="Jiang J">J Jiang</name></author><author><name sortKey="Zhang, X" uniqKey="Zhang X">X Zhang</name></author><author><name sortKey="Chen, Y" uniqKey="Chen Y">Y Chen</name></author><author><name sortKey="Wu, Y" uniqKey="Wu Y">Y Wu</name></author><author><name sortKey="Zhou, Zh" uniqKey="Zhou Z">ZH Zhou</name></author><author><name sortKey="Chang, Z" uniqKey="Chang Z">Z Chang</name></author><author><name sortKey="Sui, S" uniqKey="Sui S">S Sui</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Sohn, J" uniqKey="Sohn J">J Sohn</name></author><author><name sortKey="Grant, Ra" uniqKey="Grant R">RA Grant</name></author><author><name sortKey="Sauer, Rt" uniqKey="Sauer R">RT Sauer</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Wilken, C" uniqKey="Wilken C">C Wilken</name></author><author><name sortKey="Kitzing, K" uniqKey="Kitzing K">K Kitzing</name></author><author><name sortKey="Kurzbauer, R" uniqKey="Kurzbauer R">R Kurzbauer</name></author><author><name sortKey="Ehrmann, Mm" uniqKey="Ehrmann M">MM Ehrmann</name></author><author><name sortKey="Clausen, T" uniqKey="Clausen T">T Clausen</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Mohamedmohaideen, Nn" uniqKey="Mohamedmohaideen N">NN MohamedMohaideen</name></author><author><name sortKey="Palaninathan, Sk" uniqKey="Palaninathan S">SK Palaninathan</name></author><author><name sortKey="Morin, Pm" uniqKey="Morin P">PM Morin</name></author><author><name sortKey="Williams, Bj" uniqKey="Williams B">BJ Williams</name></author><author><name sortKey="Braunstein, M" uniqKey="Braunstein M">M Braunstein</name></author><author><name sortKey="Tichy, Se" uniqKey="Tichy S">SE Tichy</name></author><author><name sortKey="Locker, J" uniqKey="Locker J">J Locker</name></author><author><name sortKey="Russell, Dh" uniqKey="Russell D">DH Russell</name></author><author><name sortKey="Jacobs, Wr" uniqKey="Jacobs W">WR Jacobs</name></author><author><name sortKey="Sacchettini, Jc" uniqKey="Sacchettini J">JC Sacchettini</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Huston, Wm" uniqKey="Huston W">WM Huston</name></author><author><name sortKey="Tyndall, Jda" uniqKey="Tyndall J">JDA Tyndall</name></author><author><name sortKey="Lott, Wb" uniqKey="Lott W">WB Lott</name></author><author><name sortKey="Stansfield, Sh" uniqKey="Stansfield S">SH Stansfield</name></author><author><name sortKey="Timms, P" uniqKey="Timms P">P Timms</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Finn, Rd" uniqKey="Finn R">RD Finn</name></author><author><name sortKey="Clements, J" uniqKey="Clements J">J Clements</name></author><author><name sortKey="Eddy, Sr" uniqKey="Eddy S">SR Eddy</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Shi, J" uniqKey="Shi J">J Shi</name></author><author><name sortKey="Blundell, Tl" uniqKey="Blundell T">TL Blundell</name></author><author><name sortKey="Mizuguchi, K" uniqKey="Mizuguchi K">K Mizuguchi</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Sali, A" uniqKey="Sali A">A Sali</name></author><author><name sortKey="Blundell, Tl" uniqKey="Blundell T">TL Blundell</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Ko, J" uniqKey="Ko J">J Ko</name></author><author><name sortKey="Lee, D" uniqKey="Lee D">D Lee</name></author><author><name sortKey="Park, H" uniqKey="Park H">H Park</name></author><author><name sortKey="Coutsias, Ea" uniqKey="Coutsias E">EA Coutsias</name></author><author><name sortKey="Lee, J" uniqKey="Lee J">J Lee</name></author><author><name sortKey="Seok, C" uniqKey="Seok C">C Seok</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Laskowski, Ra" uniqKey="Laskowski R">RA Laskowski</name></author><author><name sortKey="Macarthur, Mw" uniqKey="Macarthur M">MW MacArthur</name></author><author><name sortKey="Moss, Ds" uniqKey="Moss D">DS Moss</name></author><author><name sortKey="Thornton, Jm" uniqKey="Thornton J">JM Thornton</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Huston, Wm" uniqKey="Huston W">WM Huston</name></author><author><name sortKey="Swedberg, Je" uniqKey="Swedberg J">JE Swedberg</name></author><author><name sortKey="Harris, Jm" uniqKey="Harris J">JM Harris</name></author><author><name sortKey="Walsh, Tp" uniqKey="Walsh T">TP Walsh</name></author><author><name sortKey="Mathews, Sa" uniqKey="Mathews S">SA Mathews</name></author><author><name sortKey="Timms, P" uniqKey="Timms P">P Timms</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Berry, Lj" uniqKey="Berry L">LJ Berry</name></author><author><name sortKey="Hickey, Dk" uniqKey="Hickey D">DK Hickey</name></author><author><name sortKey="Skelding, Ka" uniqKey="Skelding K">KA Skelding</name></author><author><name sortKey="Bao, S" uniqKey="Bao S">S Bao</name></author><author><name sortKey="Rendina, Am" uniqKey="Rendina A">AM Rendina</name></author><author><name sortKey="Hansbro, Pm" uniqKey="Hansbro P">PM Hansbro</name></author><author><name sortKey="Gockel, Cm" uniqKey="Gockel C">CM Gockel</name></author><author><name sortKey="Beagley, Kw" uniqKey="Beagley K">KW Beagley</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Hauske, P" uniqKey="Hauske P">P Hauske</name></author><author><name sortKey="Meltzer, M" uniqKey="Meltzer M">M Meltzer</name></author><author><name sortKey="Ottmann, C" uniqKey="Ottmann C">C Ottmann</name></author><author><name sortKey="Krojer, T" uniqKey="Krojer T">T Krojer</name></author><author><name sortKey="Clausen, T" uniqKey="Clausen T">T Clausen</name></author><author><name sortKey="Ehrmann, Mm" uniqKey="Ehrmann M">MM Ehrmann</name></author><author><name sortKey="Kaiser, M" uniqKey="Kaiser M">M Kaiser</name></author></analytic></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">Cell Mol Biol Lett</journal-id><journal-id journal-id-type="iso-abbrev">Cell. Mol. Biol. Lett</journal-id><journal-title-group><journal-title>Cellular & Molecular Biology Letters</journal-title></journal-title-group><issn pub-type="ppub">1425-8153</issn><issn pub-type="epub">1689-1392</issn><publisher><publisher-name>Springer Vienna</publisher-name><publisher-loc>Vienna</publisher-loc></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">24036669</article-id><article-id pub-id-type="pmc">6275972</article-id><article-id pub-id-type="publisher-id">103</article-id><article-id pub-id-type="doi">10.2478/s11658-013-0103-2</article-id><article-categories><subj-group subj-group-type="heading"><subject>Research Article</subject></subj-group></article-categories><title-group><article-title>Proteolytic activation of <italic>Chlamydia trachomatis</italic> HTRA is mediated by PDZ1 domain interactions with protease domain loops L3 and LC and beta strand β5</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Marsh</surname><given-names>James W.</given-names></name><xref ref-type="aff" rid="Aff1">1</xref></contrib><contrib contrib-type="author"><name><surname>Lott</surname><given-names>William B.</given-names></name><xref ref-type="aff" rid="Aff1">1</xref></contrib><contrib contrib-type="author" corresp="yes"><name><surname>Tyndall</surname><given-names>Joel D. A.</given-names></name><address><phone>+64 3 4797293</phone><fax>+64 3 4797034</fax><email>joel.tyndall@otago.ac.nz</email></address><xref ref-type="aff" rid="Aff2">2</xref></contrib><contrib contrib-type="author" corresp="yes"><name><surname>Huston</surname><given-names>Wilhelmina Willa M.</given-names></name><address><phone>+61 7 3138 6258</phone><fax>+61 7 3138 6030</fax><email>w.huston@qut.edu.au</email></address><xref ref-type="aff" rid="Aff1">1</xref></contrib><aff id="Aff1"><label>1</label><institution-wrap><institution-id institution-id-type="GRID">grid.1024.7</institution-id><institution-id institution-id-type="ISNI">0000000089150953</institution-id><institution>Institute of Health and Biomedical Innovation (IHBI),</institution><institution>Queensland University of Technology (QUT),</institution></institution-wrap>60 Musk Avenue, Kelvin Grove, Queensland Australia 4059</aff><aff id="Aff2"><label>2</label><institution-wrap><institution-id institution-id-type="GRID">grid.29980.3a</institution-id><institution-id institution-id-type="ISNI">0000000419367830</institution-id><institution>National School of Pharmacy,</institution><institution>University of Otago,</institution></institution-wrap>PO Box 56, Dunedin, New Zealand 9054</aff></contrib-group><pub-date pub-type="epub"><day>13</day><month>9</month><year>2013</year></pub-date><pub-date pub-type="collection"><month>12</month><year>2013</year></pub-date><volume>18</volume><issue>4</issue><fpage>522</fpage><lpage>537</lpage><history><date date-type="received"><day>14</day><month>6</month><year>2013</year></date><date date-type="accepted"><day>9</day><month>9</month><year>2013</year></date></history><permissions><copyright-statement>© Versita Warsaw and Springer-Verlag Wien 2013</copyright-statement></permissions><abstract id="Abs1"><p><italic>Chlamydia trachomatis</italic> is a bacterial pathogen responsible for one of the most prevalent sexually transmitted infections worldwide. Its unique development cycle has limited our understanding of its pathogenic mechanisms. However, CtHtrA has recently been identified as a potential <italic>C. trachomatis</italic> virulence factor. CtHtrA is a tightly regulated quality control protein with a monomeric structural unit comprised of a chymotrypsin-like protease domain and two PDZ domains. Activation of proteolytic activity relies on the C-terminus of the substrate allosterically binding to the PDZ1 domain, which triggers subsequent conformational change and oligomerization of the protein into 24-mers enabling proteolysis. This activation is mediated by a cascade of precise structural arrangements, but the specific CtHtrA residues and structural elements required to facilitate activation are unknown. Using <italic>in vitro</italic> analysis guided by homology modeling, we show that the mutation of residues Arg362 and Arg224, predicted to disrupt the interaction between the CtHtrA PDZ1 domain and loop L3, and between loop L3 and loop LD, respectively, are critical for the activation of proteolytic activity. We also demonstrate that mutation to residues Arg299 and Lys160, predicted to disrupt PDZ1 domain interactions with protease loop LC and strand β5, are also able to influence proteolysis, implying their involvement in the CtHtrA mechanism of activation. This is the first investigation of protease loop LC and strand β5 with respect to their potential interactions with the PDZ1 domain. Given their high level of conservation in bacterial HtrA, these structural elements may be equally significant in the activation mechanism of DegP and other HtrA family members.</p></abstract><kwd-group xml:lang="en"><title>Key words</title><kwd><italic>Chlamydia</italic></kwd><kwd>HtrA</kwd><kwd>DegP</kwd><kwd>Protease</kwd><kwd>Oligomerization</kwd></kwd-group><custom-meta-group><custom-meta><meta-name>issue-copyright-statement</meta-name><meta-value>© Versita Warsaw and Springer-Verlag Wien 2013</meta-value></custom-meta></custom-meta-group></article-meta></front><back><glossary><title>Abbreviations used</title><def-list><def-item><term>CD</term><def><p>circular dichroism</p></def></def-item><def-item><term>CtHtrA</term><def><p><italic>Chlamydia trachomatis</italic> high temperature requirement A</p></def></def-item><def-item><term>MCA</term><def><p>7-methoxycoumarin-4-acetic acid</p></def></def-item><def-item><term>MOMP</term><def><p>major outer membrane protein</p></def></def-item><def-item><term>MRW</term><def><p>mean residue weight</p></def></def-item><def-item><term>OmpA</term><def><p>outer membrane protein A</p></def></def-item><def-item><term>PDZ</term><def><p>PSD-95/Dics-Large/ZO-1</p></def></def-item><def-item><term>PmpC</term><def><p>polymorphic membrane protein C</p></def></def-item><def-item><term>pNA</term><def><p><italic>para</italic>-nitroalinine</p></def></def-item><def-item><term>SDM</term><def><p>site-directed mutagenesis</p></def></def-item><def-item><term>SDS-PAGE</term><def><p>sodium dodecyl sulphate polyacrylamide gel electrophoresis</p></def></def-item></def-list></glossary><ref-list id="Bib1"><title>References</title><ref id="CR1"><label>1.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Stephens</surname><given-names>RS</given-names></name></person-group><article-title>The cellular paradigm of chlamydial pathogenesis</article-title><source>Trends Microbiol.</source><year>2003</year><volume>11</volume><fpage>44</fpage><lpage>51</lpage><pub-id pub-id-type="doi">10.1016/S0966-842X(02)00011-2</pub-id><pub-id pub-id-type="pmid">12526854</pub-id></element-citation></ref><ref id="CR2"><label>2.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Low</surname><given-names>N</given-names></name></person-group><article-title>Incidence of severe reproductive tract complications associated with diagnosed genital chlamydial infection: the Uppsala Women’s Cohort Study</article-title><source>Sex. Transm. Infect.</source><year>2006</year><volume>82</volume><fpage>212</fpage><lpage>218</lpage><pub-id pub-id-type="doi">10.1136/sti.2005.017186</pub-id><pub-id pub-id-type="pmid">16731670</pub-id></element-citation></ref><ref id="CR3"><label>3.</label><mixed-citation publication-type="other">Huston, W.M., Theodoropoulos, C., Mathews, S.A. and Timms, P. <italic>Chlamydia trachomatis</italic> responds to heat shock, penicillin-induced persistence, and IFNgamma persistence by altering levels of the extracytoplasmic stress response protease HtrA. <bold>BMC Microbiol.</bold><underline>8</underline> (2008).</mixed-citation></ref><ref id="CR4"><label>4.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Pedersen</surname><given-names>LL</given-names></name><name><surname>Radulic</surname><given-names>MM</given-names></name><name><surname>Doric</surname><given-names>MM</given-names></name><name><surname>Kwaik</surname><given-names>YYA</given-names></name></person-group><article-title>HtrA homologue of <italic>Legionella pneumophila</italic>: an indispensable element for intracellular infection of mammalian but not protozoan cells</article-title><source>Infect. Immun.</source><year>2001</year><volume>69</volume><fpage>2569</fpage><lpage>2579</lpage><pub-id pub-id-type="doi">10.1128/IAI.69.4.2569-2579.2001</pub-id><pub-id pub-id-type="pmid">11254621</pub-id></element-citation></ref><ref id="CR5"><label>5.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Lewis</surname><given-names>C</given-names></name><name><surname>Skovierova</surname><given-names>H</given-names></name><name><surname>Rowley</surname><given-names>G</given-names></name><name><surname>Rezuchova</surname><given-names>B</given-names></name><name><surname>Homerova</surname><given-names>D</given-names></name><name><surname>Stevenson</surname><given-names>A</given-names></name><name><surname>Spencer</surname><given-names>J</given-names></name><name><surname>Farn</surname><given-names>J</given-names></name><name><surname>Kormanec</surname><given-names>J</given-names></name><name><surname>Roberts</surname><given-names>M</given-names></name></person-group><article-title><italic>Salmonella enterica</italic> serovar Typhimurium HtrA: regulation of expression and role of the chaperone and protease activities during infection</article-title><source>Microbiology</source><year>2009</year><volume>155</volume><fpage>873</fpage><lpage>881</lpage><pub-id pub-id-type="doi">10.1099/mic.0.023754-0</pub-id><pub-id pub-id-type="pmid">19246758</pub-id></element-citation></ref><ref id="CR6"><label>6.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Hoy</surname><given-names>B</given-names></name><name><surname>Lower</surname><given-names>M</given-names></name><name><surname>Weydig</surname><given-names>C</given-names></name><name><surname>Carra</surname><given-names>G</given-names></name><name><surname>Tegtmeyer</surname><given-names>N</given-names></name><name><surname>Geppert</surname><given-names>T</given-names></name><name><surname>Schroder</surname><given-names>P</given-names></name><name><surname>Sewald</surname><given-names>N</given-names></name><name><surname>Backert</surname><given-names>S</given-names></name><name><surname>Schneider</surname><given-names>G</given-names></name><name><surname>Wessler</surname><given-names>S</given-names></name></person-group><article-title><italic>Helicobacter pylori</italic> HtrA is a new secreted virulence factor that cleaves E-cadherin to disrupt intercellular adhesion</article-title><source>EMBO Rep.</source><year>2010</year><volume>11</volume><fpage>798</fpage><lpage>804</lpage><pub-id pub-id-type="doi">10.1038/embor.2010.114</pub-id><pub-id pub-id-type="pmid">20814423</pub-id></element-citation></ref><ref id="CR7"><label>7.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Strauch</surname><given-names>KL</given-names></name><name><surname>Beckwith</surname><given-names>J</given-names></name></person-group><article-title>An <italic>Escherichia coli</italic> mutation preventing degradation of abnormal periplasmic proteins</article-title><source>Proc. Natl. Acad. Sci. U.S.A.</source><year>1988</year><volume>85</volume><fpage>1576</fpage><lpage>1580</lpage><pub-id pub-id-type="doi">10.1073/pnas.85.5.1576</pub-id><pub-id pub-id-type="pmid">3278319</pub-id></element-citation></ref><ref id="CR8"><label>8.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Lipinska</surname><given-names>BB</given-names></name><name><surname>Zylicz</surname><given-names>M</given-names></name><name><surname>Georgopoulos</surname><given-names>CC</given-names></name></person-group><article-title>The HtrA (DegP) protein, essential for <italic>Escherichia coli</italic> survival at high temperatures, is an endopeptidase</article-title><source>J. Bacteriol.</source><year>1990</year><volume>172</volume><fpage>1791</fpage><lpage>1797</lpage><pub-id pub-id-type="pmid">2180903</pub-id></element-citation></ref><ref id="CR9"><label>9.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Spiess</surname><given-names>CC</given-names></name><name><surname>Beil</surname><given-names>AA</given-names></name><name><surname>Ehrmann</surname><given-names>MM</given-names></name></person-group><article-title>A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein</article-title><source>Cell</source><year>1999</year><volume>97</volume><fpage>339</fpage><lpage>347</lpage><pub-id pub-id-type="doi">10.1016/S0092-8674(00)80743-6</pub-id><pub-id pub-id-type="pmid">10319814</pub-id></element-citation></ref><ref id="CR10"><label>10.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Baldi</surname><given-names>A</given-names></name><name><surname>De Luca</surname><given-names>A</given-names></name><name><surname>Morini</surname><given-names>M</given-names></name><name><surname>Battista</surname><given-names>T</given-names></name><name><surname>Felsani</surname><given-names>A</given-names></name><name><surname>Baldi</surname><given-names>F</given-names></name><name><surname>Catricalà</surname><given-names>C</given-names></name><name><surname>Amantea</surname><given-names>A</given-names></name><name><surname>Noonan</surname><given-names>DM</given-names></name><name><surname>Albini</surname><given-names>A</given-names></name><name><surname>Natali</surname><given-names>PG</given-names></name><name><surname>Lombardi</surname><given-names>D</given-names></name><name><surname>Paggi</surname><given-names>MG</given-names></name></person-group><article-title>The HtrA1 serine protease is down-regulated during human melanoma progression and represses growth of metastatic melanoma cells</article-title><source>Oncogene</source><year>2002</year><volume>21</volume><fpage>6684</fpage><lpage>6688</lpage><pub-id pub-id-type="doi">10.1038/sj.onc.1205911</pub-id><pub-id pub-id-type="pmid">12242667</pub-id></element-citation></ref><ref id="CR11"><label>11.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Li</surname><given-names>W</given-names></name><name><surname>Srinivasula</surname><given-names>SM</given-names></name><name><surname>Chai</surname><given-names>J</given-names></name><name><surname>Li</surname><given-names>P</given-names></name><name><surname>Wu</surname><given-names>J</given-names></name><name><surname>Zhang</surname><given-names>Z</given-names></name><name><surname>Alnemri</surname><given-names>ES</given-names></name><name><surname>Shi</surname><given-names>Y</given-names></name></person-group><article-title>Structural insights into the pro-apoptotic function of mitochondrial serine protease HtrA2/Omi</article-title><source>Nat. Struct. Biol.</source><year>2002</year><volume>9</volume><fpage>436</fpage><lpage>441</lpage><pub-id pub-id-type="doi">10.1038/nsb795</pub-id><pub-id pub-id-type="pmid">11967569</pub-id></element-citation></ref><ref id="CR12"><label>12.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Clausen</surname><given-names>T</given-names></name><name><surname>Southan</surname><given-names>C</given-names></name><name><surname>Ehrmann</surname><given-names>MM</given-names></name></person-group><article-title>The HtrA family of proteases: implications for protein composition and cell fate</article-title><source>Mol. Cell</source><year>2002</year><volume>10</volume><fpage>443</fpage><lpage>455</lpage><pub-id pub-id-type="doi">10.1016/S1097-2765(02)00658-5</pub-id><pub-id pub-id-type="pmid">12408815</pub-id></element-citation></ref><ref id="CR13"><label>13.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Grau</surname><given-names>S</given-names></name><name><surname>Baldi</surname><given-names>A</given-names></name><name><surname>Bussani</surname><given-names>R</given-names></name><name><surname>Tian</surname><given-names>X</given-names></name><name><surname>Stefanescu</surname><given-names>R</given-names></name><name><surname>Przybylski</surname><given-names>M</given-names></name><name><surname>Richards</surname><given-names>P</given-names></name><name><surname>Jones</surname><given-names>SA</given-names></name><name><surname>Shridhar</surname><given-names>V</given-names></name><name><surname>Clausen</surname><given-names>T</given-names></name><name><surname>Ehrmann</surname><given-names>MM</given-names></name></person-group><article-title>Implications of the serine protease HtrA1 in amyloid precursor protein processing</article-title><source>Proc. Natl. Acad. Sci. U. S. A.</source><year>2005</year><volume>102</volume><fpage>6021</fpage><lpage>6026</lpage><pub-id pub-id-type="doi">10.1073/pnas.0501823102</pub-id><pub-id pub-id-type="pmid">15855271</pub-id></element-citation></ref><ref id="CR14"><label>14.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Hansen</surname><given-names>G</given-names></name><name><surname>Hilgenfeld</surname><given-names>R</given-names></name></person-group><article-title>Architecture and regulation of HtrA-family proteins involved in protein quality control and stress response</article-title><source>Cell. Mol. Life Sci.</source><year>2012</year><volume>70</volume><fpage>761</fpage><lpage>775</lpage><pub-id pub-id-type="doi">10.1007/s00018-012-1076-4</pub-id><pub-id pub-id-type="pmid">22806565</pub-id></element-citation></ref><ref id="CR15"><label>15.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Rawlings</surname><given-names>ND</given-names></name><name><surname>Barrett</surname><given-names>AJ</given-names></name><name><surname>Bateman</surname><given-names>A</given-names></name></person-group><article-title>MEROPS: the peptidase database</article-title><source>Nucleic Acids Res.</source><year>2009</year><volume>38</volume><fpage>227</fpage><lpage>233</lpage><pub-id pub-id-type="doi">10.1093/nar/gkp971</pub-id></element-citation></ref><ref id="CR16"><label>16.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Spiers</surname><given-names>A</given-names></name></person-group><article-title>PDZ domains facilitate binding of high temperature requirement protease A (HtrA) and tail-specific protease (Tsp) to heterologous substrates through recognition of the small stable RNA A (ssrA)-encoded peptide</article-title><source>J. Biol. Chem.</source><year>2002</year><volume>277</volume><fpage>39443</fpage><lpage>39449</lpage><pub-id pub-id-type="doi">10.1074/jbc.M202790200</pub-id><pub-id pub-id-type="pmid">12177052</pub-id></element-citation></ref><ref id="CR17"><label>17.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Kolmar</surname><given-names>HH</given-names></name><name><surname>Waller</surname><given-names>PR</given-names></name><name><surname>Sauer</surname><given-names>RT</given-names></name></person-group><article-title>The DegP and DegQ periplasmic endoproteases of <italic>Escherichia coli</italic>: specificity for cleavage sites and substrate conformation</article-title><source>J. Bacteriol.</source><year>1996</year><volume>178</volume><fpage>5925</fpage><lpage>5929</lpage><pub-id pub-id-type="pmid">8830688</pub-id></element-citation></ref><ref id="CR18"><label>18.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Kim</surname><given-names>SS</given-names></name><name><surname>Sauer</surname><given-names>RT</given-names></name></person-group><article-title>Cage assembly of DegP protease is not required for substrate-dependent regulation of proteolytic activity or high-temperature cell survival</article-title><source>Proc. Natl. Acad. Sci. U.S.A.</source><year>2012</year><volume>109</volume><fpage>7263</fpage><lpage>7268</lpage><pub-id pub-id-type="doi">10.1073/pnas.1204791109</pub-id><pub-id pub-id-type="pmid">22529381</pub-id></element-citation></ref><ref id="CR19"><label>19.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Krojer</surname><given-names>T</given-names></name><name><surname>Garrido-Franco</surname><given-names>M</given-names></name><name><surname>Huber</surname><given-names>R</given-names></name><name><surname>Ehrmann</surname><given-names>MM</given-names></name><name><surname>Clausen</surname><given-names>T</given-names></name></person-group><article-title>Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine</article-title><source>Nature</source><year>2002</year><volume>416</volume><fpage>455</fpage><lpage>459</lpage><pub-id pub-id-type="doi">10.1038/416455a</pub-id><pub-id pub-id-type="pmid">11919638</pub-id></element-citation></ref><ref id="CR20"><label>20.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Krojer</surname><given-names>T</given-names></name><name><surname>Sawa</surname><given-names>J</given-names></name><name><surname>Huber</surname><given-names>R</given-names></name><name><surname>Clausen</surname><given-names>T</given-names></name></person-group><article-title>HtrA proteases have a conserved activation mechanism that can be triggered by distinct molecular cues</article-title><source>Nat. Struct. Mol. Biol.</source><year>2010</year><volume>17</volume><fpage>844</fpage><lpage>852</lpage><pub-id pub-id-type="doi">10.1038/nsmb.1840</pub-id><pub-id pub-id-type="pmid">20581825</pub-id></element-citation></ref><ref id="CR21"><label>21.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Clausen</surname><given-names>T</given-names></name><name><surname>Kaiser</surname><given-names>M</given-names></name><name><surname>Huber</surname><given-names>R</given-names></name><name><surname>Ehrmann</surname><given-names>MM</given-names></name></person-group><article-title>HtrA proteases: regulated proteolysis in protein quality control</article-title><source>Nat. Rev. Mol. Cell Biol.</source><year>2011</year><volume>12</volume><fpage>152</fpage><lpage>162</lpage><pub-id pub-id-type="doi">10.1038/nrm3065</pub-id><pub-id pub-id-type="pmid">21326199</pub-id></element-citation></ref><ref id="CR22"><label>22.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Jiang</surname><given-names>J</given-names></name><name><surname>Zhang</surname><given-names>X</given-names></name><name><surname>Chen</surname><given-names>Y</given-names></name><name><surname>Wu</surname><given-names>Y</given-names></name><name><surname>Zhou</surname><given-names>ZH</given-names></name><name><surname>Chang</surname><given-names>Z</given-names></name><name><surname>Sui</surname><given-names>S</given-names></name></person-group><article-title>Activation of DegP chaperone-protease via formation of large cage-like oligomers upon binding to substrate proteins</article-title><source>Proc. Natl. Acad. Sci. U.S.A.</source><year>2008</year><volume>105</volume><fpage>11939</fpage><lpage>11944</lpage><pub-id pub-id-type="doi">10.1073/pnas.0805464105</pub-id><pub-id pub-id-type="pmid">18697939</pub-id></element-citation></ref><ref id="CR23"><label>23.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Sohn</surname><given-names>J</given-names></name><name><surname>Grant</surname><given-names>RA</given-names></name><name><surname>Sauer</surname><given-names>RT</given-names></name></person-group><article-title>OMP peptides activate the DegS stresssensor protease by a relief of inhibition mechanism</article-title><source>Structure</source><year>2009</year><volume>17</volume><fpage>1411</fpage><lpage>1421</lpage><pub-id pub-id-type="doi">10.1016/j.str.2009.07.017</pub-id><pub-id pub-id-type="pmid">19836340</pub-id></element-citation></ref><ref id="CR24"><label>24.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Wilken</surname><given-names>C</given-names></name><name><surname>Kitzing</surname><given-names>K</given-names></name><name><surname>Kurzbauer</surname><given-names>R</given-names></name><name><surname>Ehrmann</surname><given-names>MM</given-names></name><name><surname>Clausen</surname><given-names>T</given-names></name></person-group><article-title>Crystal structure of the DegS stress sensor: how a PDZ domain recognizes misfolded protein and activates a protease</article-title><source>Cell</source><year>2004</year><volume>117</volume><fpage>483</fpage><lpage>494</lpage><pub-id pub-id-type="doi">10.1016/S0092-8674(04)00454-4</pub-id><pub-id pub-id-type="pmid">15137941</pub-id></element-citation></ref><ref id="CR25"><label>25.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>MohamedMohaideen</surname><given-names>NN</given-names></name><name><surname>Palaninathan</surname><given-names>SK</given-names></name><name><surname>Morin</surname><given-names>PM</given-names></name><name><surname>Williams</surname><given-names>BJ</given-names></name><name><surname>Braunstein</surname><given-names>M</given-names></name><name><surname>Tichy</surname><given-names>SE</given-names></name><name><surname>Locker</surname><given-names>J</given-names></name><name><surname>Russell</surname><given-names>DH</given-names></name><name><surname>Jacobs</surname><given-names>WR</given-names></name><name><surname>Sacchettini</surname><given-names>JC</given-names></name></person-group><article-title>Structure and function of the virulence-associated hightemperature requirement A of <italic>Mycobacterium tuberculosis</italic></article-title><source>Biochemistry</source><year>2008</year><volume>47</volume><fpage>6092</fpage><lpage>6102</lpage><pub-id pub-id-type="doi">10.1021/bi701929m</pub-id><pub-id pub-id-type="pmid">18479146</pub-id></element-citation></ref><ref id="CR26"><label>26.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Huston</surname><given-names>WM</given-names></name><name><surname>Tyndall</surname><given-names>JDA</given-names></name><name><surname>Lott</surname><given-names>WB</given-names></name><name><surname>Stansfield</surname><given-names>SH</given-names></name><name><surname>Timms</surname><given-names>P</given-names></name></person-group><article-title>Unique residues involved in activation of the multitasking protease/chaperone HtrA from <italic>Chlamydia trachomatis</italic></article-title><source>PLoS ONE</source><year>2011</year><volume>6</volume><fpage>e24547</fpage><pub-id pub-id-type="doi">10.1371/journal.pone.0024547</pub-id><pub-id pub-id-type="pmid">21931748</pub-id></element-citation></ref><ref id="CR27"><label>27.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Finn</surname><given-names>RD</given-names></name><name><surname>Clements</surname><given-names>J</given-names></name><name><surname>Eddy</surname><given-names>SR</given-names></name></person-group><article-title>HMMER web server: interactive sequence similarity searching</article-title><source>Nucleic Acids Res.</source><year>2011</year><volume>39</volume><fpage>29</fpage><lpage>37</lpage><pub-id pub-id-type="doi">10.1093/nar/gkr367</pub-id></element-citation></ref><ref id="CR28"><label>28.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Shi</surname><given-names>J</given-names></name><name><surname>Blundell</surname><given-names>TL</given-names></name><name><surname>Mizuguchi</surname><given-names>K</given-names></name></person-group><article-title>FUGUE: sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties</article-title><source>J. Mol. Biol.</source><year>2001</year><volume>310</volume><fpage>243</fpage><lpage>257</lpage><pub-id pub-id-type="doi">10.1006/jmbi.2001.4762</pub-id><pub-id pub-id-type="pmid">11419950</pub-id></element-citation></ref><ref id="CR29"><label>29.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Sali</surname><given-names>A</given-names></name><name><surname>Blundell</surname><given-names>TL</given-names></name></person-group><article-title>Comparative protein modeling by satisfaction of spatial restraints</article-title><source>J. Mol. Biol.</source><year>1993</year><volume>234</volume><fpage>779</fpage><lpage>815</lpage><pub-id pub-id-type="doi">10.1006/jmbi.1993.1626</pub-id><pub-id pub-id-type="pmid">8254673</pub-id></element-citation></ref><ref id="CR30"><label>30.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Ko</surname><given-names>J</given-names></name><name><surname>Lee</surname><given-names>D</given-names></name><name><surname>Park</surname><given-names>H</given-names></name><name><surname>Coutsias</surname><given-names>EA</given-names></name><name><surname>Lee</surname><given-names>J</given-names></name><name><surname>Seok</surname><given-names>C</given-names></name></person-group><article-title>The FALC-Loop web server for protein loop modeling</article-title><source>Nucleic Acids Res.</source><year>2011</year><volume>39</volume><fpage>210</fpage><lpage>214</lpage><pub-id pub-id-type="doi">10.1093/nar/gkr352</pub-id></element-citation></ref><ref id="CR31"><label>31.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Laskowski</surname><given-names>RA</given-names></name><name><surname>MacArthur</surname><given-names>MW</given-names></name><name><surname>Moss</surname><given-names>DS</given-names></name><name><surname>Thornton</surname><given-names>JM</given-names></name></person-group><article-title>PROCHECK: a program to check the stereochemical quality of protein structures</article-title><source>J. Appl. Crystallogr.</source><year>1993</year><volume>26</volume><fpage>283</fpage><lpage>291</lpage><pub-id pub-id-type="doi">10.1107/S0021889892009944</pub-id></element-citation></ref><ref id="CR32"><label>32.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Huston</surname><given-names>WM</given-names></name><name><surname>Swedberg</surname><given-names>JE</given-names></name><name><surname>Harris</surname><given-names>JM</given-names></name><name><surname>Walsh</surname><given-names>TP</given-names></name><name><surname>Mathews</surname><given-names>SA</given-names></name><name><surname>Timms</surname><given-names>P</given-names></name></person-group><article-title>The temperature activated HtrA protease from pathogen <italic>Chlamydia trachomatis</italic> acts as both a chaperone and protease at 37°C</article-title><source>FEBS Lett.</source><year>2007</year><volume>581</volume><fpage>3382</fpage><lpage>3386</lpage><pub-id pub-id-type="doi">10.1016/j.febslet.2007.06.039</pub-id><pub-id pub-id-type="pmid">17604025</pub-id></element-citation></ref><ref id="CR33"><label>33.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Berry</surname><given-names>LJ</given-names></name><name><surname>Hickey</surname><given-names>DK</given-names></name><name><surname>Skelding</surname><given-names>KA</given-names></name><name><surname>Bao</surname><given-names>S</given-names></name><name><surname>Rendina</surname><given-names>AM</given-names></name><name><surname>Hansbro</surname><given-names>PM</given-names></name><name><surname>Gockel</surname><given-names>CM</given-names></name><name><surname>Beagley</surname><given-names>KW</given-names></name></person-group><article-title>Transcutaneous immunisation with combined cholera toxin and CpG adjuvant protects against <italic>Chlamydia muridarum</italic> genital tract infection</article-title><source>Infect. Immun.</source><year>2004</year><volume>72</volume><fpage>1019</fpage><lpage>1028</lpage><pub-id pub-id-type="doi">10.1128/IAI.72.2.1019-1028.2004</pub-id><pub-id pub-id-type="pmid">14742549</pub-id></element-citation></ref><ref id="CR34"><label>34.</label><element-citation publication-type="journal"><person-group person-group-type="author"><name><surname>Hauske</surname><given-names>P</given-names></name><name><surname>Meltzer</surname><given-names>M</given-names></name><name><surname>Ottmann</surname><given-names>C</given-names></name><name><surname>Krojer</surname><given-names>T</given-names></name><name><surname>Clausen</surname><given-names>T</given-names></name><name><surname>Ehrmann</surname><given-names>MM</given-names></name><name><surname>Kaiser</surname><given-names>M</given-names></name></person-group><article-title>Selectivity profiling of DegP substrates and inhibitors</article-title><source>Bioorgan. Med. Chem.</source><year>2009</year><volume>17</volume><fpage>2920</fpage><lpage>2924</lpage><pub-id pub-id-type="doi">10.1016/j.bmc.2009.01.073</pub-id></element-citation></ref></ref-list></back></pmc></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/MersV1/Data/Pmc/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 0003479 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Pmc/Corpus/biblio.hfd -nk 0003479 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Sante
|area= MersV1
|flux= Pmc
|étape= Corpus
|type= RBID
|clé=
|texte=
}}
| This area was generated with Dilib version V0.6.33. |  |