3RVA
Crystal structure of organophosphorus acid anhydrolase from Alteromonas macleodii
3RVA の概要
| エントリーDOI | 10.2210/pdb3rva/pdb |
| 分子名称 | Organophosphorus acid anhydrolase, MANGANESE (II) ION, PHOSPHATE ION, ... (5 entities in total) |
| 機能のキーワード | organophosphorus acid anhydrolase, pita-bread fold, binuclear metal center, bi-functional, prolidase, nerve agents, xaa-pro dipeptides, hydrolase |
| 由来する生物種 | Alteromonas macleodii |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 51786.32 |
| 構造登録者 | Stepankova, A.,Koval, T.,Ostergaard, L.H.,Duskova, J.,Skalova, T.,Hasek, J.,Dohnalek, J. (登録日: 2011-05-06, 公開日: 2012-05-09, 最終更新日: 2024-11-27) |
| 主引用文献 | Stepankova, A.,Duskova, J.,Skalova, T.,Hasek, J.,Koval, T.,Ostergaard, L.H.,Dohnalek, J. Organophosphorus acid anhydrolase from Alteromonas macleodii: structural study and functional relationship to prolidases. Acta Crystallogr.,Sect.F, 69:346-354, 2013 Cited by PubMed Abstract: The bacterial enzyme organophosphorus acid anhydrolase (OPAA) is able to catalyze the hydrolysis of both proline dipeptides (Xaa-Pro) and several types of organophosphate (OP) compounds. The full three-dimensional structure of the manganese-dependent OPAA enzyme is presented for the first time. This enzyme, which was originally isolated from the marine bacterium Alteromonas macleodii, was prepared recombinantly in Escherichia coli. The crystal structure was determined at 1.8 Å resolution in space group C2, with unit-cell parameters a = 133.8, b = 49.2, c = 97.3 Å, β = 125.0°. The enzyme forms dimers and their existence in solution was confirmed by dynamic light scattering and size-exclusion chromatography. The enzyme shares the pita-bread fold of its C-terminal domain with related prolidases. The binuclear manganese centre is located in the active site within the pita-bread domain. Moreover, an Ni(2+) ion from purification was localized according to anomalous signal. This study presents the full structure of this enzyme with complete surroundings of the active site and provides a critical analysis of its relationship to prolidases. PubMed: 23545636DOI: 10.1107/S1744309113002674 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.8 Å) |
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