2qom: Difference between revisions

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<StructureSection load='2qom' size='340' side='right'caption='[[2qom]], [[Resolution|resolution]] 2.66&Aring;' scene=''>
<StructureSection load='2qom' size='340' side='right'caption='[[2qom]], [[Resolution|resolution]] 2.66&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2qom]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Eco57 Eco57]. 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>
<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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">espP ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83334 ECO57])</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]] 2.66&#8491;</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>
[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.
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>
From MEDLINE&reg;/PubMed&reg;, 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: Eco57]]
[[Category: Escherichia coli O157:H7]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Barnard, T J]]
[[Category: Barnard TJ]]
[[Category: Bernstein, H D]]
[[Category: Bernstein HD]]
[[Category: Buchanan, S K]]
[[Category: Buchanan SK]]
[[Category: Dautin, N]]
[[Category: Dautin N]]
[[Category: Lukacik, P]]
[[Category: Lukacik P]]
[[Category: Autotransporter]]
[[Category: Beta-barrel]]
[[Category: Beta-domain]]
[[Category: Hydrolase]]
[[Category: Outer membrane protein]]
[[Category: Protease]]
[[Category: Secreted]]
[[Category: Serine protease]]
[[Category: Transmembrane]]
[[Category: Virulence]]
[[Category: Zymogen]]

Latest revision as of 09:17, 21 February 2024

The crystal structure of the E.coli EspP autotransporter Beta-domain.

2qom, resolution 2.66Å

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