3H1E
Crystal structure of Mg(2+) and BeH(3)(-)-bound CheY of Helicobacter pylori
3H1E の概要
エントリーDOI | 10.2210/pdb3h1e/pdb |
関連するPDBエントリー | 3GWG 3H1F 3H1G |
分子名称 | Chemotaxis protein cheY homolog, MAGNESIUM ION, BERYLLIUM TRIFLUORIDE ION, ... (5 entities in total) |
機能のキーワード | chemotaxis, bef3-bound chey, cytoplasm, flagellar rotation, magnesium, metal-binding, phosphoprotein, two-component regulatory system, signaling protein |
由来する生物種 | Helicobacter pylori |
細胞内の位置 | Cytoplasm (Potential): P71403 |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 14555.27 |
構造登録者 | |
主引用文献 | Lam, K.H.,Ling, T.K.,Au, S.W. Crystal structure of activated CheY1 from Helicobacter pylori. J.Bacteriol., 192:2324-2334, 2010 Cited by PubMed Abstract: 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. PubMed: 20207758DOI: 10.1128/JB.00603-09 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.4 Å) |
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