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2OBM

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

Summary for 2OBM
Entry DOI10.2210/pdb2obm/pdb
Related2OBL
DescriptorEscN, CALCIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
Functional Keywordsatpase, hydrolase
Biological sourceEscherichia coli O127:H6
Total number of polymer chains1
Total formula weight38134.68
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: 2023-08-30)
Primary citationZarivach, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.25 Å)
Structure validation

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数据于2025-10-15公开中

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