Journal
PROTEIN SCIENCE
Volume 19, Issue 5, Pages 1091-1096Publisher
WILEY
DOI: 10.1002/pro.382
Keywords
type III secretion; Salmonella; crystal structure; InvA
Categories
Funding
- Canadian Commonwealth Scholarship Program
- Canadian Institutes for Health Research
- Howard Hughes Medical Institute
- Canada Foundation for Innovation
- Michael Smith Foundation for Health Research
- NSERC
- NRC
- University of Saskatchewan
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InvA is a prominent inner-membrane component of the Salmonella type Ill 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.
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