2X49

Crystal structure of the C-terminal domain of InvA

Summary for 2X49

• Entry DOI: 10.2210/pdb2x49/pdb
• Related: 2X4A
• Descriptor: INVASION PROTEIN INVA, MERCURY (II) ION, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: protein transport, transport, pathogenesis
• Biological source: SALMONELLA ENTERICA SUBSP. ENTERICA SEROVAR TYPHIMURIUM
• Cellular location: Cell inner membrane; Multi-pass membrane protein (Potential): P0A1I3
• Total number of polymer chains: 1
• Total formula weight: 38941.08

Authors

Worrall, L.J.,Vuckovic, M.,Strynadka, N.C.J. (deposition date: 2010-01-28, release date: 2010-03-31, Last modification date: 2024-05-08)

Primary citation

Worrall, 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

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

Experimental method

X-RAY DIFFRACTION (1.5 Å)