6RKO
Cryo-EM structure of the E. coli cytochrome bd-I oxidase at 2.68 A resolution
Summary for 6RKO
| Entry DOI | 10.2210/pdb6rko/pdb |
| EMDB information | 4908 |
| Descriptor | Cytochrome bd-I ubiquinol oxidase subunit 2, Cytochrome bd-I ubiquinol oxidase subunit 1, Uncharacterized protein YnhF, ... (10 entities in total) |
| Functional Keywords | oxidoreductase cytochrome bd oxidase bd oxidase oxidase, membrane protein |
| Biological source | Escherichia coli (strain K12) More |
| Total number of polymer chains | 4 |
| Total formula weight | 113443.77 |
| Authors | Safarian, S.,Hahn, A.,Kuehlbrandt, W.,Michel, H. (deposition date: 2019-04-30, release date: 2019-10-16, Last modification date: 2024-05-22) |
| Primary citation | 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 Cited by 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: 31604309DOI: 10.1126/science.aay0967 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.68 Å) |
Structure validation
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