6RX4
THE STRUCTURE OF BD OXIDASE FROM ESCHERICHIA COLI
6RX4 の概要
| エントリーDOI | 10.2210/pdb6rx4/pdb |
| EMDBエントリー | 10049 |
| 分子名称 | Cytochrome bd-I ubiquinol oxidase subunit 1, Cytochrome bd-I ubiquinol oxidase subunit 2, Cytochrome bd-I ubiquinol oxidase subunit X, ... (9 entities in total) |
| 機能のキーワード | bd oxidase, terminal oxidase, oxidoreductase |
| 由来する生物種 | Escherichia coli (strain K12) 詳細 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 110346.59 |
| 構造登録者 | Rasmussen, T.,Boettcher, B.,Thesseling, A.,Friedrich, T. (登録日: 2019-06-07, 公開日: 2019-11-20, 最終更新日: 2024-05-22) |
| 主引用文献 | Thesseling, A.,Rasmussen, T.,Burschel, S.,Wohlwend, D.,Kagi, J.,Muller, R.,Bottcher, B.,Friedrich, T. Homologous bd oxidases share the same architecture but differ in mechanism. Nat Commun, 10:5138-5138, 2019 Cited by PubMed Abstract: Cytochrome bd oxidases are terminal reductases of bacterial and archaeal respiratory chains. The enzyme couples the oxidation of ubiquinol or menaquinol with the reduction of dioxygen to water, thus contributing to the generation of the protonmotive force. Here, we determine the structure of the Escherichia coli bd oxidase treated with the specific inhibitor aurachin by cryo-electron microscopy (cryo-EM). The major subunits CydA and CydB are related by a pseudo two fold symmetry. The heme b and d cofactors are found in CydA, while ubiquinone-8 is bound at the homologous positions in CydB to stabilize its structure. The architecture of the E. coli enzyme is highly similar to that of Geobacillus thermodenitrificans, however, the positions of heme b and d are interchanged, and a common oxygen channel is blocked by a fourth subunit and substituted by a more narrow, alternative channel. Thus, with the same overall fold, the homologous enzymes exhibit a different mechanism. PubMed: 31723136DOI: 10.1038/s41467-019-13122-4 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (3.3 Å) |
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