2qom
From Proteopedia
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| - | [[Image:2qom.jpg|left|200px]] | + | [[Image:2qom.jpg|left|200px]] |
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| - | '''The crystal structure of the E.coli EspP autotransporter Beta-domain.''' | + | {{Structure |
| + | |PDB= 2qom |SIZE=350|CAPTION= <scene name='initialview01'>2qom</scene>, resolution 2.66Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= espP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | }} | ||
| + | |||
| + | '''The crystal structure of the E.coli EspP autotransporter Beta-domain.''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2QOM is a [ | + | 2QOM is a [[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== | ==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:// | + | 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://www.ncbi.nlm.nih.gov/pubmed/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 Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:27:54 2008'' |
Revision as of 16:27, 20 March 2008
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| , resolution 2.66Å | |||||||
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| Gene: | espP (Escherichia coli) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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