2OBM

Structural and biochemical analysis of a prototypical ATPase from the type III secretion system of pathogenic bacteria

2OBM の概要

• エントリーDOI: 10.2210/pdb2obm/pdb
• 関連するPDBエントリー: 2OBL
• 分子名称: EscN, CALCIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: atpase, hydrolase
• 由来する生物種: Escherichia coli O127:H6
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 38134.68

構造登録者

Zarivach, R.,Vuckovic, M.,Deng, W.,Finlay, B.B.,Strynadka, N.C.J. (登録日: 2006-12-19, 公開日: 2007-01-30, 最終更新日: 2023-08-30)

主引用文献

Zarivach, R.,Vuckovic, M.,Deng, W.,Finlay, B.B.,Strynadka, N.C.
Structural analysis of a prototypical ATPase from the type III secretion system.
Nat.Struct.Mol.Biol., 14:131-137, 2007

PubMed Abstract: The type III secretion system (T3SS) ATPase is the conserved and essential inner-membrane component involved in the initial stages of selective secretion of specialized T3SS virulence effector proteins from the bacterial cytoplasm through to the infected host cell, a process crucial to subsequent pathogenicity. Here we present the 1.8-A-resolution crystal structure of the catalytic domain of the prototypical T3SS ATPase EscN from enteropathogenic Escherichia coli (EPEC). Along with in vitro and in vivo mutational analysis, our data show that the T3SS ATPases share similarity with the F1 ATPases but have important structural and sequence differences that dictate their unique secretory role. We also show that T3SS ATPase activity is dependent on EscN oligomerization and describe the molecular features and possible functional implications of a hexameric ring model.

PubMed: 17237797
DOI: 10.1038/nsmb1196

実験手法

X-RAY DIFFRACTION (2.25 Å)