2obl

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

spinqualitylabelsall models 2obl, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2obl is a 1 chain structure with sequence from Escherichia coli O127:H6 str. E2348/69. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8Å Ligands: ACT, CA, IMD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function B7UMA6_ECO27 Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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