4G2S

Crystal structure of a Salmonella type III secretion system protein

Summary for 4G2S

• Entry DOI: 10.2210/pdb4g2s/pdb
• Related: 4G08 4G1I
• Descriptor: Protein prgH, CALCIUM ION (3 entities in total)
• Functional Keywords: fha domain, cell invasion
• Biological source: Salmonella enterica subsp. enterica serovar Typhimurium (Salmonella typhimurium)
• Cellular location: Cell membrane; Single-pass membrane protein (Potential): P41783
• Total number of polymer chains: 6
• Total formula weight: 72084.51

Authors

Worrall, L.J.,Vuckovic, M.,Strynadka, N.C.J. (deposition date: 2012-07-12, release date: 2013-05-15, 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

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

X-RAY DIFFRACTION (1.858 Å)