2qom
From Proteopedia
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The crystal structure of the E.coli EspP autotransporter Beta-domain.
Overview
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.
About this Structure
2QOM is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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
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