3GR1

Periplasmic domain of the T3SS inner membrane protein PrgH from S.typhimurium (fragment 170-392)

Summary for 3GR1

• Entry DOI: 10.2210/pdb3gr1/pdb
• Related: 3GR0 3GR5
• Descriptor: Protein prgH (1 entity in total)
• Functional Keywords: type iii secretion system, inner membrane protein, cell membrane, membrane, transmembrane, virulence, membrane protein
• Biological source: Salmonella typhimurium
• Cellular location: Cell membrane ; Single-pass membrane protein : P41783
• Total number of polymer chains: 8
• Total formula weight: 211783.90

Authors

Yip, C.K.,Vockovic, M.,Yu, A.C.,Strynadka, N.C.J. (deposition date: 2009-03-24, release date: 2009-05-19, Last modification date: 2023-09-06)

Primary citation

Spreter, T.,Yip, C.K.,Sanowar, S.,Andre, I.,Kimbrough, T.G.,Vuckovic, M.,Pfuetzner, R.A.,Deng, W.,Yu, A.C.,Finlay, B.B.,Baker, D.,Miller, S.I.,Strynadka, N.C.
A conserved structural motif mediates formation of the periplasmic rings in the type III secretion system.
Nat.Struct.Mol.Biol., 16:468-476, 2009

PubMed Abstract: The type III secretion system (T3SS) is a macromolecular 'injectisome' that allows bacterial pathogens to transport virulence proteins into the eukaryotic host cell. This macromolecular complex is composed of connected ring-like structures that span both bacterial membranes. The crystal structures of the periplasmic domain of the outer membrane secretin EscC and the inner membrane protein PrgH reveal the conservation of a modular fold among the three proteins that form the outer membrane and inner membrane rings of the T3SS. This leads to the hypothesis that this conserved fold provides a common ring-building motif that allows for the assembly of the variably sized outer membrane and inner membrane rings characteristic of the T3SS. Using an integrated structural and experimental approach, we generated ring models for the periplasmic domain of EscC and placed them in the context of the assembled T3SS, providing evidence for direct interaction between the outer membrane and inner membrane ring components and an unprecedented span of the outer membrane secretin.

PubMed: 19396170
DOI: 10.1038/nsmb.1603

Experimental method

X-RAY DIFFRACTION (2.8 Å)