1M57
Structure of cytochrome c oxidase from Rhodobacter sphaeroides (EQ(I-286) mutant))
1M57 の概要
| エントリーDOI | 10.2210/pdb1m57/pdb |
| 関連するPDBエントリー | 1M56 |
| 分子名称 | CYTOCHROME C OXIDASE, COPPER (II) ION, MAGNESIUM ION, ... (10 entities in total) |
| 機能のキーワード | membrane protein, oxidoreductase |
| 由来する生物種 | Rhodobacter sphaeroides 詳細 |
| 細胞内の位置 | Cell membrane; Multi-pass membrane protein: P33517 Q03736 Membrane; Multi-pass membrane protein (By similarity): P84153 |
| タンパク質・核酸の鎖数 | 8 |
| 化学式量合計 | 269270.77 |
| 構造登録者 | Svensson-Ek, M.,Abramson, J.,Larsson, G.,Tornroth, S.,Brezezinski, P.,Iwata, S. (登録日: 2002-07-08, 公開日: 2002-08-28, 最終更新日: 2024-10-30) |
| 主引用文献 | Svensson-Ek, M.,Abramson, J.,Larsson, G.,Tornroth, S.,Brzezinski, P.,Iwata, S. The X-ray crystal structures of wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides. J.Mol.Biol., 321:329-339, 2002 Cited by PubMed Abstract: The structure of cytochrome c oxidase from Rhodobacter sphaeroides has been solved at 2.3/2.8A (anisotropic resolution). This high-resolution structure revealed atomic details of a bacterial terminal oxidase including water molecule positions and a potential oxygen pathway, which has not been reported in other oxidase structures. A comparative study of the wild-type and the EQ(I-286) mutant enzyme revealed structural rearrangements around E(I-286) that could be crucial for proton transfer in this enzyme. In the structure of the mutant enzyme, EQ(I-286), which cannot transfer protons during oxygen reduction, the side-chain of Q(I-286) does not have the hydrogen bond to the carbonyl oxygen of M(I-107) that is seen in the wild-type structure. Furthermore, the Q(I-286) mutant has a different arrangement of water molecules and residues in the vicinity of the Q side-chain. These differences between the structures could reflect conformational changes that take place upon deprotonation of E(I-286) during turnover of the wild-type enzyme, which could be part of the proton-pumping machinery of the enzyme. PubMed: 12144789DOI: 10.1016/S0022-2836(02)00619-8 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3 Å) |
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