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2qom
From Proteopedia
(New page: 200px<br /><applet load="2qom" size="350" color="white" frame="true" align="right" spinBox="true" caption="2qom, resolution 2.66Å" /> '''The crystal structur...) |
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caption="2qom, resolution 2.66Å" /> | caption="2qom, resolution 2.66Å" /> | ||
'''The crystal structure of the E.coli EspP autotransporter Beta-domain.'''<br /> | '''The crystal structure of the E.coli EspP autotransporter Beta-domain.'''<br /> | ||
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| + | ==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== | ==About this Structure== | ||
2QOM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QOM OCA]. | 2QOM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QOM 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17994105 17994105] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: zymogen]] | [[Category: zymogen]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jan 31 10:59:13 2008'' |
Revision as of 08:59, 31 January 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 Jan 31 10:59:13 2008
