- PDB-4g2s: Crystal structure of a Salmonella type III secretion system protein -
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Basic information
Entry
Database: PDB / ID: 4g2s
Title
Crystal structure of a Salmonella type III secretion system protein
Components
Protein prgH
Keywords
CELL INVASION / FHA domain
Function / homology
Type III secretion system, PrgH/EprH / Type III secretion system, PrgH/EprH-like / Type III secretion system protein PrgH-EprH (PrgH) / Tumour Suppressor Smad4 - #20 / Tumour Suppressor Smad4 / Sandwich / Mainly Beta / plasma membrane / Protein PrgH
Journal: PLoS Pathog / Year: 2013 Title: A refined model of the prototypical Salmonella SPI-1 T3SS basal body reveals the molecular basis for its assembly. Authors: Julien R C Bergeron / Liam J Worrall / Nikolaos G Sgourakis / Frank DiMaio / Richard A Pfuetzner / Heather B Felise / Marija Vuckovic / Angel C Yu / Samuel I Miller / David Baker / Natalie C J Strynadka / 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 ...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.