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| | ==The crystal structure of Ail, the attachment invasion locus protein of Yersinia pestis== | | ==The crystal structure of Ail, the attachment invasion locus protein of Yersinia pestis== |
| - | <StructureSection load='3qra' size='340' side='right' caption='[[3qra]], [[Resolution|resolution]] 1.80Å' scene=''> | + | <StructureSection load='3qra' size='340' side='right'caption='[[3qra]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3qra]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_pestis"_(lehmann_and_neumann_1896)_migula_1900 "bacillus pestis" (lehmann and neumann 1896) migula 1900]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QRA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QRA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3qra]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Yersinia_pestis Yersinia pestis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QRA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QRA FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=C8E:(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE'>C8E</scene></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]] 1.801Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3qrc|3qrc]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C8E:(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE'>C8E</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ail, YPO2905 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=632 "Bacillus pestis" (Lehmann and Neumann 1896) Migula 1900])</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=3qra FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qra OCA], [https://pdbe.org/3qra PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qra RCSB], [https://www.ebi.ac.uk/pdbsum/3qra PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qra 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=3qra FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qra OCA], [http://pdbe.org/3qra PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3qra RCSB], [http://www.ebi.ac.uk/pdbsum/3qra PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3qra ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/Q8D0Z7_YERPE Q8D0Z7_YERPE] |
| - | Ail is an outer membrane protein from Yersinia pestis that is highly expressed in a rodent model of bubonic plague, making it a good candidate for vaccine development. Ail is important for attaching to host cells and evading host immune responses, facilitating rapid progression of a plague infection. Binding to host cells is important for injection of cytotoxic Yersinia outer proteins. To learn more about how Ail mediates adhesion, we solved two high-resolution crystal structures of Ail, with no ligand bound and in complex with a heparin analog called sucrose octasulfate. We identified multiple adhesion targets, including laminin and heparin, and showed that a 40 kDa domain of laminin called LG4-5 specifically binds to Ail. We also evaluated the contribution of laminin to delivery of Yops to HEp-2 cells. This work constitutes a structural description of how a bacterial outer membrane protein uses a multivalent approach to bind host cells.
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| - | Structural Insights into Ail-Mediated Adhesion in Yersinia pestis.,Yamashita S, Lukacik P, Barnard TJ, Noinaj N, Felek S, Tsang TM, Krukonis ES, Hinnebusch BJ, Buchanan SK Structure. 2011 Nov 9;19(11):1672-82. PMID:22078566<ref>PMID:22078566</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 3qra" style="background-color:#fffaf0;"></div>
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| - | == References ==
| + | |
| - | <references/>
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Buchanan, S K]] | + | [[Category: Large Structures]] |
| - | [[Category: Lukacik, P]] | + | [[Category: Yersinia pestis]] |
| - | [[Category: Noinaj, N]] | + | [[Category: Buchanan SK]] |
| - | [[Category: Yamashita, S]] | + | [[Category: Lukacik P]] |
| - | [[Category: Attachment and invasion virulence]] | + | [[Category: Noinaj N]] |
| - | [[Category: Beta-barrel protein]] | + | [[Category: Yamashita S]] |
| - | [[Category: Cell invasion]]
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| - | [[Category: Heparin]]
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| - | [[Category: Laminin]]
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