7OSE
cytochrome bd-II type oxidase with bound aurachin D
Summary for 7OSE
| Entry DOI | 10.2210/pdb7ose/pdb |
| EMDB information | 13048 |
| Descriptor | 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) |
| Functional Keywords | terminal oxidase, q-loop, inhibitor binding, membrane protein |
| Biological source | Escherichia coli BW25113 More |
| Total number of polymer chains | 6 |
| Total formula weight | 213941.23 |
| Authors | Grauel, A.,Kaegi, J.,Rasmussen, T.,Wohlwend, D.,Boettcher, B.,Friedrich, T. (deposition date: 2021-06-08, release date: 2021-11-17, Last modification date: 2023-09-20) |
| Primary citation | 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 Cited by 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: 34764272DOI: 10.1038/s41467-021-26835-2 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3 Å) |
Structure validation
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