7OSE

cytochrome bd-II type oxidase with bound aurachin D

7OSE の概要

• エントリーDOI: 10.2210/pdb7ose/pdb
• EMDBエントリー: 13048
• 分子名称: Cytochrome bd-II ubiquinol oxidase subunit 1, Cytochrome bd-II ubiquinol oxidase subunit 2, Putative cytochrome bd-II ubiquinol oxidase subunit AppX, ... (8 entities in total)
• 機能のキーワード: terminal oxidase, q-loop, inhibitor binding, membrane protein
• 由来する生物種: Escherichia coli BW25113; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 213941.23

構造登録者

Grauel, A.,Kaegi, J.,Rasmussen, T.,Wohlwend, D.,Boettcher, B.,Friedrich, T. (登録日: 2021-06-08, 公開日: 2021-11-17, 最終更新日: 2023-09-20)

主引用文献

Grauel, A.,Kagi, J.,Rasmussen, T.,Makarchuk, I.,Oppermann, S.,Moumbock, A.F.A.,Wohlwend, D.,Muller, R.,Melin, F.,Gunther, S.,Hellwig, P.,Bottcher, B.,Friedrich, T.
Structure of Escherichia coli cytochrome bd-II type oxidase with bound aurachin D.
Nat Commun, 12:6498-6498, 2021

PubMed Abstract: Cytochrome bd quinol:O oxidoreductases are respiratory terminal oxidases so far only identified in prokaryotes, including several pathogenic bacteria. Escherichia coli contains two bd oxidases of which only the bd-I type is structurally characterized. Here, we report the structure of the Escherichia coli cytochrome bd-II type oxidase with the bound inhibitor aurachin D as obtained by electron cryo-microscopy at 3 Å resolution. The oxidase consists of subunits AppB, C and X that show an architecture similar to that of bd-I. The three heme cofactors are found in AppC, while AppB is stabilized by a structural ubiquinone-8 at the homologous positions. A fourth subunit present in bd-I is lacking in bd-II. Accordingly, heme b is exposed to the membrane but heme d embedded within the protein and showing an unexpectedly high redox potential is the catalytically active centre. The structure of the Q-loop is fully resolved, revealing the specific aurachin binding.

PubMed: 34764272
DOI: 10.1038/s41467-021-26835-2

実験手法

ELECTRON MICROSCOPY (3 Å)