3J1W

A refined model of the prototypical Salmonella typhimurium T3SS basal body reveals the molecular basis for its assembly

Summary for 3J1W

• Entry DOI: 10.2210/pdb3j1w/pdb
• Related: 3J1V 3J1X 4G08 4G1I
• EMDB information: 1875
• Descriptor: Protein PrgH (1 entity in total)
• Functional Keywords: t3ss, cell invasion
• Biological source: Salmonella enterica subsp. enterica serovar Typhimurium
• Total number of polymer chains: 24
• Total formula weight: 278928.82

Authors

Sgourakis, N.G.,Worrall, L.J.,Strynadka, N.C.J.,Baker, D. (deposition date: 2012-07-10, release date: 2013-05-22, Last modification date: 2024-02-21)

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

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: 23633951
DOI: 10.1371/journal.ppat.1003307

Experimental method

ELECTRON MICROSCOPY (11.7 Å)