Structural highlights
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
