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| <StructureSection load='5y2d' size='340' side='right'caption='[[5y2d]], [[Resolution|resolution]] 3.70Å' scene=''> | | <StructureSection load='5y2d' size='340' side='right'caption='[[5y2d]], [[Resolution|resolution]] 3.70Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[5y2d]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Campylobacter_pylori Campylobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y2D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Y2D FirstGlance]. <br> | | <table><tr><td colspan='2'>[[5y2d]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori_26695 Helicobacter pylori 26695]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y2D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5Y2D FirstGlance]. <br> |
| </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hp1018/19 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=85962 Campylobacter pylori])</td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.7000985Å</td></tr> |
| <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidase_Do Peptidase Do], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.107 3.4.21.107] </span></td></tr>
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5y2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y2d OCA], [https://pdbe.org/5y2d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5y2d RCSB], [https://www.ebi.ac.uk/pdbsum/5y2d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5y2d ProSAT]</span></td></tr> |
| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5y2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y2d OCA], [http://pdbe.org/5y2d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5y2d RCSB], [http://www.ebi.ac.uk/pdbsum/5y2d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5y2d ProSAT]</span></td></tr> | |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
| | == Function == |
| == Publication Abstract from PubMed == | | [https://www.uniprot.org/uniprot/G2J5T2_HELPY G2J5T2_HELPY] |
| Knowledge of the molecular mechanisms of specific bacterial virulence factors can significantly contribute to antibacterial drug discovery. Helicobacter pylori is a Gram-negative microaerophilic bacterium that infects almost half of the world's population, leading to gastric disorders and even gastric cancer. H. pylori expresses a series of virulence factors in the host, among which high-temperature requirement A (HpHtrA) is a newly identified serine protease secreted by H. pylori. HpHtrA cleaves the extracellular domain of the epithelial cell surface adhesion protein E-cadherin and disrupts gastric epithelial cell junctions, allowing H. pylori to access the intercellular space. Here we report the first crystal structure of HpHtrA at 3.0 A resolution. The structure revealed a new type of HtrA protease trimer stabilized by unique N-terminal domain swapping distinct from other known HtrA homologs. We further observed that truncation of the N terminus completely abrogates HpHtrA trimer formation as well as protease activity. In the presence of unfolded substrate, HpHtrA assembled into cage-like 12-mers or 24-mers. Combining crystallographic, biochemical, and mutagenic data, we propose a mechanistic model of how HpHtrA recognizes and cleaves the well-folded E-cadherin substrate. Our study provides a fundamental basis for the development of anti-H. pylori agents by using a previously uncharacterized HtrA protease as a target.
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| The unique trimeric assembly of the virulence factor HtrA from Helicobacter pylori occurs via N-terminal domain swapping.,Zhang Z, Huang Q, Tao X, Song G, Zheng P, Li H, Sun H, Xia W J Biol Chem. 2019 May 17;294(20):7990-8000. doi: 10.1074/jbc.RA119.007387. Epub, 2019 Apr 1. PMID:30936204<ref>PMID:30936204</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
| |
| <div class="pdbe-citations 5y2d" style="background-color:#fffaf0;"></div>
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| == References ==
| |
| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Campylobacter pylori]] | | [[Category: Helicobacter pylori 26695]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Peptidase Do]]
| | [[Category: Huang Q]] |
| [[Category: Huang, Q]] | | [[Category: Tao X]] |
| [[Category: Tao, X]] | | [[Category: Zhang Z]] |
| [[Category: Zhang, Z]] | |
| [[Category: Hydrolase]]
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| [[Category: Serine protease]]
| |