6RKO

Cryo-EM structure of the E. coli cytochrome bd-I oxidase at 2.68 A resolution

6RKO の概要

• エントリーDOI: 10.2210/pdb6rko/pdb
• EMDBエントリー: 4908
• 分子名称: Cytochrome bd-I ubiquinol oxidase subunit 2, Cytochrome bd-I ubiquinol oxidase subunit 1, Uncharacterized protein YnhF, ... (10 entities in total)
• 機能のキーワード: oxidoreductase cytochrome bd oxidase bd oxidase oxidase, membrane protein
• 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: 113443.77

構造登録者

Safarian, S.,Hahn, A.,Kuehlbrandt, W.,Michel, H. (登録日: 2019-04-30, 公開日: 2019-10-16, 最終更新日: 2024-05-22)

主引用文献

Safarian, S.,Hahn, A.,Mills, D.J.,Radloff, M.,Eisinger, M.L.,Nikolaev, A.,Meier-Credo, J.,Melin, F.,Miyoshi, H.,Gennis, R.B.,Sakamoto, J.,Langer, J.D.,Hellwig, P.,Kuhlbrandt, W.,Michel, H.
Active site rearrangement and structural divergence in prokaryotic respiratory oxidases.
Science, 366:100-104, 2019

PubMed Abstract: Cytochrome bd-type quinol oxidases catalyze the reduction of molecular oxygen to water in the respiratory chain of many human-pathogenic bacteria. They are structurally unrelated to mitochondrial cytochrome c oxidases and are therefore a prime target for the development of antimicrobial drugs. We determined the structure of the cytochrome bd-I oxidase by single-particle cryo-electron microscopy to a resolution of 2.7 angstroms. Our structure contains a previously unknown accessory subunit CydH, the L-subfamily-specific Q-loop domain, a structural ubiquinone-8 cofactor, an active-site density interpreted as dioxygen, distinct water-filled proton channels, and an oxygen-conducting pathway. Comparison with another cytochrome bd oxidase reveals structural divergence in the family, including rearrangement of high-spin hemes and conformational adaption of a transmembrane helix to generate a distinct oxygen-binding site.

PubMed: 31604309
DOI: 10.1126/science.aay0967

実験手法

ELECTRON MICROSCOPY (2.68 Å)