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-Structure paper
Title | Active site rearrangement and structural divergence in prokaryotic respiratory oxidases. |
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Journal, issue, pages | Science, Vol. 366, Issue 6461, Page 100-104, Year 2019 |
Publish date | Oct 4, 2019 |
Authors | S Safarian / A Hahn / D J Mills / M Radloff / M L Eisinger / A Nikolaev / J Meier-Credo / F Melin / H Miyoshi / R B Gennis / J Sakamoto / J D Langer / P Hellwig / W Kühlbrandt / H Michel / |
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 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. |
External links | Science / PubMed:31604309 |
Methods | EM (single particle) |
Resolution | 2.68 Å |
Structure data | |
Chemicals | ChemComp-UQ8: ChemComp-POV: ChemComp-HDD: ChemComp-HEB: ChemComp-OXY: ChemComp-HOH: |
Source |
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Keywords | MEMBRANE PROTEIN / Oxidoreductase Cytochrome bd oxidase bd oxidase Oxidase |