2OBL

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

Summary for 2OBL

• Entry DOI: 10.2210/pdb2obl/pdb
• Related: 2OBM
• Descriptor: EscN, CALCIUM ION, ACETATE ION, ... (5 entities in total)
• Functional Keywords: atpase, hydrolase
• Biological source: Escherichia coli O127:H6
• Total number of polymer chains: 1
• Total formula weight: 37835.61

Authors

Zarivach, R.,Vuckovic, M.,Deng, W.,Finlay, B.B.,Strynadka, N.C.J. (deposition date: 2006-12-19, release date: 2007-01-30, Last modification date: 2023-12-27)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.8 Å)