5IY5
Electron transfer complex of cytochrome c and cytochrome c oxidase at 2.0 angstrom resolution
5IY5 の概要
| エントリーDOI | 10.2210/pdb5iy5/pdb |
| 関連するPDBエントリー | 5B3S |
| 分子名称 | Cytochrome c oxidase subunit 1, Cytochrome c oxidase subunit 7A1, mitochondrial, Cytochrome c oxidase subunit 7B, mitochondrial, ... (32 entities in total) |
| 機能のキーワード | oxidoreductase |
| 由来する生物種 | Bos taurus (Bovine) 詳細 |
| タンパク質・核酸の鎖数 | 28 |
| 化学式量合計 | 456564.57 |
| 構造登録者 | Shimada, S.,Baba, J.,Aoe, S.,Shimada, A.,Yamashita, E.,Tsukihara, T. (登録日: 2016-03-24, 公開日: 2017-01-11, 最終更新日: 2023-11-08) |
| 主引用文献 | Shimada, S.,Shinzawa-Itoh, K.,Baba, J.,Aoe, S.,Shimada, A.,Yamashita, E.,Kang, J.,Tateno, M.,Yoshikawa, S.,Tsukihara, T. Complex structure of cytochrome c-cytochrome c oxidase reveals a novel protein-protein interaction mode EMBO J., 36:291-300, 2017 Cited by PubMed Abstract: Mitochondrial cytochrome c oxidase (CcO) transfers electrons from cytochrome c (Cyt.c) to O to generate HO, a process coupled to proton pumping. To elucidate the mechanism of electron transfer, we determined the structure of the mammalian Cyt.c-CcO complex at 2.0-Å resolution and identified an electron transfer pathway from Cyt.c to CcO. The specific interaction between Cyt.c and CcO is stabilized by a few electrostatic interactions between side chains within a small contact surface area. Between the two proteins are three water layers with a long inter-molecular span, one of which lies between the other two layers without significant direct interaction with either protein. Cyt.c undergoes large structural fluctuations, using the interacting regions with CcO as a fulcrum. These features of the protein-protein interaction at the docking interface represent the first known example of a new class of protein-protein interaction, which we term "soft and specific". This interaction is likely to contribute to the rapid association/dissociation of the Cyt.c-CcO complex, which facilitates the sequential supply of four electrons for the O reduction reaction. PubMed: 27979921DOI: 10.15252/embj.201695021 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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