3h1f

Crystal structure of CheY mutant D53A of Helicobacter pyloriCrystal structure of CheY mutant D53A of Helicobacter pylori

Structural highlights 3h1f is a 1 chain structure with sequence from Helicobacter pylori 26695. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.2Å Ligands: , Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CHEY1_HELPY Chemotactic response regulator protein that modulates the rotation direction of bacterial flagellar motors. Plays an important role in the colonization and infection of Helicobacter pylori (PubMed:10722597). Upon phosphorylation by CheA, interacts with the flagellar motor protein FliM to cause clockwise flagellar rotation and bacterial reversals, as opposed to straight swimming when CheY1 is not phosphorylated (PubMed:20207758). 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 Chemotaxis is an important virulence factor for Helicobacter pylori colonization and infection. The chemotactic system of H. pylori is marked by the presence of multiple response regulators: CheY1, one CheY-like-containing CheA protein (CheAY2), and three CheV proteins. Recent studies have demonstrated that these molecules play unique roles in the chemotactic signal transduction mechanisms of H. pylori. Here we report the crystal structures of BeF(3(-)-activated CheY1 from H. pylori resolved to 2.4 A. Structural comparison of CheY1 with active-site residues of BeF3(-)-bound CheY from Escherichia coli and fluorescence quenching experiments revealed the importance of Thr84 in the phosphotransfer reaction. Complementation assays using various nonchemotactic E. coli mutants and pull-down experiments demonstrated that CheY1 displays differential association with the flagellar motor in E. coli. The structural rearrangement of helix 5 and the C-terminal loop in CheY1 provide a different interaction surface for FliM. On the other hand, interaction of the CheA-P2 domain with CheY1, but not with CheY2/CheV proteins, underlines the preferential recognition of CheY1 by CheA in the phosphotransfer reaction. Our results provide the first structural insight into the features of the H. pylori chemotactic system as a model for Epsilonproteobacteria. Crystal structure of activated CheY1 from Helicobacter pylori.,Lam KH, Ling TK, Au SW J Bacteriol. 2010 May;192(9):2324-34. Epub 2010 Mar 5. PMID:20207758 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Chemotaxis protein 3D structures

spinqualitylabelsall models 3h1f, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image