3LW9

Structure of a Cytoplasmic Domain of Salmonella InvA

Summary for 3LW9

• Entry DOI: 10.2210/pdb3lw9/pdb
• Descriptor: Invasion protein invA (2 entities in total)
• Functional Keywords: inva, type iii secretion, salmonella, virulence, bacterial pathogenesis, cell inner membrane, cell membrane, membrane, protein transport, transmembrane, transport
• Biological source: Salmonella enterica subsp. enterica serovar Typhimurium
• Cellular location: Cell inner membrane ; Multi- pass membrane protein : P0A1I3
• Total number of polymer chains: 2
• Total formula weight: 39681.92

Authors

Stebbins, C.E.,Lilic, M.,Quezada, C.M. (deposition date: 2010-02-23, release date: 2010-05-26, Last modification date: 2021-10-13)

Primary citation

Lilic, M.,Quezada, C.M.,Stebbins, C.E.
A conserved domain in type III secretion links the cytoplasmic domain of InvA to elements of the basal body.
Acta Crystallogr.,Sect.D, 66:709-713, 2010

PubMed Abstract: Protein type III secretion systems (T3SSs) are organic nanosyringes that achieve an energy-dependent translocation of bacterial proteins through the two membranes of Gram-negative organisms. Examples include the pathogenic systems of animals, plants and symbiotic bacteria that inject factors into eukaryotic cells, and the flagellar export system that secretes flagellin. T3SSs possess a core of several membrane-associated proteins that are conserved across all known bacterial species that use this system. The Salmonella protein InvA is one of the most highly conserved proteins of this core of critical T3SS components. The crystal structure of a C-terminal domain of InvA reveals an unexpected homology to domains that have been repeatedly found as building blocks of other elements of the T3SS apparatus. This suggests the surprising hypothesis that evolution has produced a significant component of the apparatus structure through a series of gene-duplication and gene-rearrangement events.

PubMed: 20516623
DOI: 10.1107/S0907444910010796

Experimental method

X-RAY DIFFRACTION (1.85 Å)