2qom: Difference between revisions
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'''The crystal structure of the E.coli EspP autotransporter Beta-domain.''' | '''The crystal structure of the E.coli EspP autotransporter Beta-domain.''' | ||
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[[Category: Dautin, N.]] | [[Category: Dautin, N.]] | ||
[[Category: Lukacik, P.]] | [[Category: Lukacik, P.]] | ||
[[Category: | [[Category: Autotransporter]] | ||
[[Category: | [[Category: Beta-barrel]] | ||
[[Category: | [[Category: Beta-domain]] | ||
[[Category: | [[Category: Hydrolase]] | ||
[[Category: | [[Category: Outer membrane protein]] | ||
[[Category: | [[Category: Plasmid]] | ||
[[Category: | [[Category: Protease]] | ||
[[Category: | [[Category: Secreted]] | ||
[[Category: | [[Category: Serine protease]] | ||
[[Category: | [[Category: Transmembrane]] | ||
[[Category: | [[Category: Virulence]] | ||
[[Category: | [[Category: Zymogen]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 15:19:11 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 12:19, 4 May 2008
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 Page seeded by OCA on Sun May 4 15:19:11 2008
