5tcr | pdb_00005tcr

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Atomic model of the Salmonella SPI-1 type III secretion injectisome basal body proteins InvG, PrgH, and PrgK

spinqualitylabelsall models 5tcr, resolution 6.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5tcr is a 63 chain structure with sequence from Salmonella enterica subsp. enterica serovar typhimurium. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 5tcp, 5tcq Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Warning: this is a large structure, and loading might take a long time or not happen at all. Function [INVG_SALTY] Involved in the invasion of the cells of the intestinal epithelium. Could be necessary for the export of invasion related determinants. [PRGH_SALTY] Required for invasion of epithelial cells. [PRGK_SALTY] Required for invasion of epithelial cells. Could be involved in protein secretion. Publication Abstract from PubMed The type III secretion (T3S) injectisome is a specialized protein nanomachine that is critical for the pathogenicity of many Gram-negative bacteria, including purveyors of plague, typhoid fever, whooping cough, sexually transmitted infections and major nosocomial infections. This syringe-shaped 3.5-MDa macromolecular assembly spans both bacterial membranes and that of the infected host cell. The internal channel formed by the injectisome allows for the direct delivery of partially unfolded virulence effectors into the host cytoplasm. The structural foundation of the injectisome is the basal body, a molecular lock-nut structure composed predominantly of three proteins that form highly oligomerized concentric rings spanning the inner and outer membranes. Here we present the structure of the prototypical Salmonella enterica serovar Typhimurium pathogenicity island 1 basal body, determined using single-particle cryo-electron microscopy, with the inner-membrane-ring and outer-membrane-ring oligomers defined at 4.3 A and 3.6 A resolution, respectively. This work presents the first, to our knowledge, high-resolution structural characterization of the major components of the basal body in the assembled state, including that of the widespread class of outer-membrane portals known as secretins. Near-atomic-resolution cryo-EM analysis of the Salmonella T3S injectisome basal body.,Worrall LJ, Hong C, Vuckovic M, Deng W, Bergeron JR, Majewski DD, Huang RK, Spreter T, Finlay BB, Yu Z, Strynadka NC Nature. 2016 Dec 14. doi: 10.1038/nature20576. PMID:27974800 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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