Structural highlights
FunctionINVA_SALTY Involved in the invasion of the cells of the intestinal epithelium. Could be involved in the translocation of the InvE protein. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedInvA 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. Crystal structure of the C-terminal domain of the Salmonella type III secretion system export apparatus protein InvA.,Worrall LJ, Vuckovic M, Strynadka NC Protein Sci. 2010 Mar 19. PMID:20306492[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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