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Protein Sci. 2010 May;19(5):1091-6. doi: 10.1002/pro.382.

Crystal structure of the C-terminal domain of the Salmonella type III secretion system export apparatus protein InvA.

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1
Centre for Blood Research, Department of Biochemistry and Molecular Biology, University of British Columbia, Life Sciences Centre, British Columbia, Canada V6T 1Z3.

Abstract

InvA is a prominent inner-membrane component of the Salmonella type III secretion system (T3SS) apparatus, which is responsible for regulating virulence protein export in pathogenic bacteria. InvA is made up of an N-terminal integral membrane domain and a C-terminal cytoplasmic domain that is proposed to form part of a docking platform for the soluble export apparatus proteins notably the T3SS ATPase InvC. Here, we report the novel crystal structure of the C-terminal domain of Salmonella InvA which shows a compact structure composed of four subdomains. The overall structure is unique although the first and second subdomains exhibit structural similarity to the peripheral stalk of the A/V-type ATPase and a ring building motif found in other T3SS proteins respectively.

PMID:
20306492
PMCID:
PMC2868250
DOI:
10.1002/pro.382
[Indexed for MEDLINE]
Free PMC Article
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