3TJA
Crystal structure of Helicobacter pylori UreE in the apo form
3TJA の概要
| エントリーDOI | 10.2210/pdb3tja/pdb |
| 関連するPDBエントリー | 3TJ8 3TJ9 |
| 分子名称 | Urease accessory protein ureE, SULFATE ION, CHLORIDE ION, ... (4 entities in total) |
| 機能のキーワード | metal binding protein |
| 由来する生物種 | Helicobacter pylori |
| 細胞内の位置 | Cytoplasm: Q09064 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 78169.89 |
| 構造登録者 | Banaszak, K.,Bellucci, M.,Zambelli, B.,Rypniewski, W.R.,Ciurli, S. (登録日: 2011-08-24, 公開日: 2011-11-02, 最終更新日: 2023-09-13) |
| 主引用文献 | Banaszak, K.,Martin-Diaconescu, V.,Bellucci, M.,Zambelli, B.,Rypniewski, W.,Maroney, M.J.,Ciurli, S. Crystallographic and X-ray absorption spectroscopic characterization of Helicobacter pylori UreE bound to Ni2+ and Zn2+ reveals a role for the disordered C-terminal arm in metal trafficking. Biochem.J., 441:1017-1026, 2012 Cited by PubMed Abstract: The survival and growth of the pathogen Helicobacter pylori in the gastric acidic environment is ensured by the activity of urease, an enzyme containing two essential Ni²⁺ ions in the active site. The metallo-chaperone UreE facilitates in vivo Ni²⁺ insertion into the apoenzyme. Crystals of apo-HpUreE (H. pylori UreE) and its Ni⁺- and Zn⁺-bound forms were obtained from protein solutions in the absence and presence of the metal ions. The crystal structures of the homodimeric protein, determined at 2.00 Å (apo), 1.59 Å (Ni²⁺) and 2.52 Å (Zn²⁺) resolution, show the conserved proximal and solvent-exposed His¹⁰² residues from two adjacent monomers invariably involved in metal binding. The C-terminal regions of the apoprotein are disordered in the crystal, but acquire significant ordering in the presence of the metal ions due to the binding of His¹⁵². The analysis of X-ray absorption spectral data obtained using solutions of Ni²⁺- and Zn²⁺-bound HpUreE provided accurate information of the metal-ion environment in the absence of solid-state effects. These results reveal the role of the histidine residues at the protein C-terminus in metal-ion binding, and the mutual influence of protein framework and metal-ion stereo-electronic properties in establishing co-ordination number and geometry leading to metal selectivity. PubMed: 22010876DOI: 10.1042/BJ20111659 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2 Å) |
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