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2qom

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[[Image:2qom.jpg|left|200px]]
[[Image:2qom.jpg|left|200px]]
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{{Structure
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|PDB= 2qom |SIZE=350|CAPTION= <scene name='initialview01'>2qom</scene>, resolution 2.66&Aring;
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|GENE= espP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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{{STRUCTURE_2qom| PDB=2qom | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qom FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qom OCA], [http://www.ebi.ac.uk/pdbsum/2qom PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2qom RCSB]</span>
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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.]]
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[[Category: autotransporter]]
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[[Category: Autotransporter]]
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[[Category: beta-barrel]]
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[[Category: Beta-barrel]]
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[[Category: beta-domain]]
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[[Category: Beta-domain]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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[[Category: outer membrane protein]]
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[[Category: Outer membrane protein]]
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[[Category: plasmid]]
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[[Category: Plasmid]]
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[[Category: protease]]
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[[Category: Protease]]
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[[Category: secreted]]
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[[Category: Secreted]]
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[[Category: serine protease]]
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[[Category: Serine protease]]
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[[Category: transmembrane]]
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[[Category: Transmembrane]]
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[[Category: virulence]]
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[[Category: Virulence]]
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[[Category: zymogen]]
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[[Category: Zymogen]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 15:19:11 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:51:32 2008''
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Revision as of 12:19, 4 May 2008

Template:STRUCTURE 2qom

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

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