3GR5

Periplasmic domain of the outer membrane secretin EscC from enteropathogenic E.coli (EPEC)

3GR5 の概要

• エントリーDOI: 10.2210/pdb3gr5/pdb
• 関連するPDBエントリー: 3GR0 3GR1
• 分子名称: EscC, SULFATE ION (3 entities in total)
• 機能のキーワード: secretin, type iii secretion system, outer membrane, transport, membrane protein
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell outer membrane (By similarity): O52135
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18145.50

構造登録者

Yip, C.K.,Vockovic, M.,Strynadka, N.C.J. (登録日: 2009-03-24, 公開日: 2009-05-19, 最終更新日: 2024-11-27)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.05 Å)