2obl
From Proteopedia
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'''Structural and biochemical analysis of a prototypical ATPase from the type III secretion system of pathogenic bacteria''' | '''Structural and biochemical analysis of a prototypical ATPase from the type III secretion system of pathogenic bacteria''' | ||
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[[Category: Vuckovic, M.]] | [[Category: Vuckovic, M.]] | ||
[[Category: Zarivach, R.]] | [[Category: Zarivach, R.]] | ||
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Revision as of 07:33, 4 May 2008
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. 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 Page seeded by OCA on Sun May 4 10:33:48 2008
