+検索条件
-Structure paper
タイトル | Structure of Escherichia coli cytochrome bd-II type oxidase with bound aurachin D. |
---|---|
ジャーナル・号・ページ | Nat Commun, Vol. 12, Issue 1, Page 6498, Year 2021 |
掲載日 | 2021年11月11日 |
著者 | Antonia Grauel / Jan Kägi / Tim Rasmussen / Iryna Makarchuk / Sabrina Oppermann / Aurélien F A Moumbock / Daniel Wohlwend / Rolf Müller / Frederic Melin / Stefan Günther / Petra Hellwig / Bettina Böttcher / Thorsten Friedrich / |
PubMed 要旨 | 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 ...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. |
リンク | Nat Commun / PubMed:34764272 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.0 Å |
構造データ | EMDB-13048, PDB-7ose: |
化合物 | ChemComp-HEB: ChemComp-HDD: ChemComp-0NI: ChemComp-UQ8: ChemComp-HOH: |
由来 |
|
キーワード | MEMBRANE PROTEIN / terminal oxidase / Q-loop / inhibitor binding |