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-Structure paper
タイトル | Structure of Escherichia coli cytochrome bd-II type oxidase with bound aurachin D. |
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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 |
![]() | 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. |
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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 |
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![]() | MEMBRANE PROTEIN / terminal oxidase / Q-loop / inhibitor binding |