2obl

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spinqualitylabelsall models 2obl, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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

Overview

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.

About this Structure

2OBL is a Single protein structure of sequence from Escherichia coli with , and as ligands. Full crystallographic information is available from OCA.

Reference

Structural analysis of a prototypical ATPase from the type III secretion system., Zarivach R, Vuckovic M, Deng W, Finlay BB, Strynadka NC, Nat Struct Mol Biol. 2007 Feb;14(2):131-7. Epub 2007 Jan 21. PMID:17237797

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