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2X4A

Crystal structure of the C-terminal domain of InvA

Summary for 2X4A
Entry DOI10.2210/pdb2x4a/pdb
Related2X49
DescriptorINVASION PROTEIN INVA, 3-CYCLOHEXYL-1-PROPYLSULFONIC ACID, PHOSPHATE ION, ... (4 entities in total)
Functional Keywordsprotein transport, transport, pathogenesis
Biological sourceSALMONELLA ENTERICA SUBSP. ENTERICA SEROVAR TYPHIMURIUM
Cellular locationCell inner membrane; Multi-pass membrane protein (Potential): P0A1I3
Total number of polymer chains1
Total formula weight38564.29
Authors
Worrall, L.J.,Vuckovic, M.,Strynadka, N.C.J. (deposition date: 2010-01-28, release date: 2010-05-05, Last modification date: 2023-12-20)
Primary citationWorrall, L.J.,Vuckovic, M.,Strynadka, N.C.J.
Crystal Structure of the C-Terminal Domain of the Salmonella Type III Secretion System Export Apparatus Protein Inva.
Protein Sci., 19:1091-, 2010
Cited by
PubMed 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.
PubMed: 20306492
DOI: 10.1002/PRO.382
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.54 Å)
Structure validation

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