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A conserved structural motif mediates formation of the periplasmic rings in the type III secretion system.

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.

journal_name

Nat Struct Mol Biol

journal_title

Nature structural & molecular biology

authors

Spreter T,Yip CK,Sanowar S,André I,Kimbrough TG,Vuckovic M,Pfuetzner RA,Deng W,Yu AC,Finlay BB,Baker D,Miller SI,Strynadka NC

doi

10.1038/nsmb.1603

subject

Has Abstract

pub_date

2009-05-01 00:00:00

pages

468-76

issue

5

eissn

1545-9993

issn

1545-9985

pii

nsmb.1603

journal_volume

16

pub_type

杂志文章

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