2qom
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Autotransporters are virulence factors produced by Gram-negative bacteria. | + | 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== | ==About this Structure== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Barnard, T | + | [[Category: Barnard, T J.]] |
| - | [[Category: Bernstein, H | + | [[Category: Bernstein, H D.]] |
| - | [[Category: Buchanan, S | + | [[Category: Buchanan, S K.]] |
[[Category: Dautin, N.]] | [[Category: Dautin, N.]] | ||
[[Category: Lukacik, P.]] | [[Category: Lukacik, P.]] | ||
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[[Category: zymogen]] | [[Category: zymogen]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:41:04 2008'' |
Revision as of 16:41, 21 February 2008
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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
Page seeded by OCA on Thu Feb 21 18:41:04 2008
