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2qom

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Revision as of 07:31, 25 October 2017

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

Structural highlights

2qom is a 2 chain structure with sequence from Eco57. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	espP (ECO57)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Brunder W, Schmidt H, Karch H. EspP, a novel extracellular serine protease of enterohaemorrhagic Escherichia coli O157:H7 cleaves human coagulation factor V. Mol Microbiol. 1997 May;24(4):767-78. PMID:9194704
↑ Szabady RL, Peterson JH, Skillman KM, Bernstein HD. An unusual signal peptide facilitates late steps in the biogenesis of a bacterial autotransporter. Proc Natl Acad Sci U S A. 2005 Jan 4;102(1):221-6. Epub 2004 Dec 22. PMID:15615856 doi:http://dx.doi.org/10.1073/pnas.0406055102
↑ Barnard TJ, Dautin N, Lukacik P, Bernstein HD, Buchanan SK. Autotransporter structure reveals intra-barrel cleavage followed by conformational changes. Nat Struct Mol Biol. 2007 Dec;14(12):1214-20. Epub 2007 Nov 11. PMID:17994105 doi:10.1038/nsmb1322

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2qom"

@@ Line 1: / Line 1: @@
 ==The crystal structure of the E.coli EspP autotransporter Beta-domain.==
 <StructureSection load='2qom' size='340' side='right' caption='[[2qom]], [[Resolution|resolution]] 2.66&Aring;' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[2qom]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2QOM FirstGlance]. <br>
 </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">espP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83334 ECO57])</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=2qom FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qom OCA], [http://pdbe.org/2qom PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2qom RCSB], [http://www.ebi.ac.uk/pdbsum/2qom PDBsum]</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=2qom FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qom OCA], [http://pdbe.org/2qom PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2qom RCSB], [http://www.ebi.ac.uk/pdbsum/2qom PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2qom ProSAT]</span></td></tr>
 </table>
 == Function ==

2qom

From Proteopedia

Revision as of 07:31, 25 October 2017

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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