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2qom
From Proteopedia
(Difference between revisions)
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<StructureSection load='2qom' size='340' side='right'caption='[[2qom]], [[Resolution|resolution]] 2.66Å' scene=''> | <StructureSection load='2qom' size='340' side='right'caption='[[2qom]], [[Resolution|resolution]] 2.66Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2qom]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2qom]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QOM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QOM FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.66Å</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=2qom FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qom OCA], [https://pdbe.org/2qom PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qom RCSB], [https://www.ebi.ac.uk/pdbsum/2qom PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qom ProSAT]</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=2qom FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qom OCA], [https://pdbe.org/2qom PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qom RCSB], [https://www.ebi.ac.uk/pdbsum/2qom PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qom ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/ESPP_ECO57 ESPP_ECO57] Serine protease capable of cleaving pepsin A and human coagulation factor V, which may contribute to the mucosal hemorrhage observed in hemorrhagic colitis.<ref>PMID:9194704</ref> <ref>PMID:15615856</ref> | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2qom ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2qom ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Autotransporters are virulence factors produced by Gram-negative bacteria. They consist of two domains, an N-terminal 'passenger' domain and a C-terminal beta-domain. beta-domains form beta-barrel structures in the outer membrane while passenger domains are translocated into the extracellular space. In some autotransporters, the two domains are separated by proteolytic cleavage. Using X-ray crystallography, we solved the 2.7-A structure of the post-cleavage state of the beta-domain of EspP, an autotransporter produced by Escherichia coli strain O157:H7. The structure consists of a 12-stranded beta-barrel with the passenger domain-beta-domain cleavage junction located inside the barrel pore, approximately midway between the extracellular and periplasmic surfaces of the outer membrane. The structure reveals an unprecedented intra-barrel cleavage mechanism and suggests that two conformational changes occur in the beta-domain after cleavage, one conferring increased stability on the beta-domain and another restricting access to the barrel pore. | ||
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| - | Autotransporter structure reveals intra-barrel cleavage followed by conformational changes.,Barnard TJ, Dautin N, Lukacik P, Bernstein HD, Buchanan SK Nat Struct Mol Biol. 2007 Dec;14(12):1214-20. Epub 2007 Nov 11. PMID:17994105<ref>PMID:17994105</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 2qom" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Escherichia coli O157:H7]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Barnard | + | [[Category: Barnard TJ]] |
| - | [[Category: Bernstein | + | [[Category: Bernstein HD]] |
| - | [[Category: Buchanan | + | [[Category: Buchanan SK]] |
| - | [[Category: Dautin | + | [[Category: Dautin N]] |
| - | [[Category: Lukacik | + | [[Category: Lukacik P]] |
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Current revision
The crystal structure of the E.coli EspP autotransporter Beta-domain.
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