4G08
Crystal structure of the periplasmic domain of InvG
Summary for 4G08
| Entry DOI | 10.2210/pdb4g08/pdb |
| Related | 3J1V 4G1I 4G2S |
| Descriptor | Protein InvG (2 entities in total) |
| Functional Keywords | ring-building motif, protein secretion, prgh, cell invasion |
| Biological source | Salmonella enterica subsp. enterica serovar Typhimurium (Salmonella typhimurium) |
| Total number of polymer chains | 1 |
| Total formula weight | 17838.30 |
| Authors | Bergeron, J.R.C.,Strynadka, N.C.J. (deposition date: 2012-07-09, release date: 2013-05-08, Last modification date: 2024-02-28) |
| Primary citation | Bergeron, J.R.,Worrall, L.J.,Sgourakis, N.G.,Dimaio, F.,Pfuetzner, R.A.,Felise, H.B.,Vuckovic, M.,Yu, A.C.,Miller, S.I.,Baker, D.,Strynadka, N.C. A Refined Model of the Prototypical Salmonella SPI-1 T3SS Basal Body Reveals the Molecular Basis for Its Assembly. Plos Pathog., 9:e1003307-e1003307, 2013 Cited by PubMed Abstract: The T3SS injectisome is a syringe-shaped macromolecular assembly found in pathogenic Gram-negative bacteria that allows for the direct delivery of virulence effectors into host cells. It is composed of a "basal body", a lock-nut structure spanning both bacterial membranes, and a "needle" that protrudes away from the bacterial surface. A hollow channel spans throughout the apparatus, permitting the translocation of effector proteins from the bacterial cytosol to the host plasma membrane. The basal body is composed largely of three membrane-embedded proteins that form oligomerized concentric rings. Here, we report the crystal structures of three domains of the prototypical Salmonella SPI-1 basal body, and use a new approach incorporating symmetric flexible backbone docking and EM data to produce a model for their oligomeric assembly. The obtained models, validated by biochemical and in vivo assays, reveal the molecular details of the interactions driving basal body assembly, and notably demonstrate a conserved oligomerization mechanism. PubMed: 23633951DOI: 10.1371/journal.ppat.1003307 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.801 Å) |
Structure validation
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