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TitleActive site rearrangement and structural divergence in prokaryotic respiratory oxidases.
Journal, issue, pagesScience, Vol. 366, Issue 6461, Page 100-104, Year 2019
Publish dateOct 4, 2019
AuthorsS 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 AbstractCytochrome 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 linksScience / PubMed:31604309
MethodsEM (single particle)
Resolution2.68 Å
Structure data

4908

6rko

EMDB-4908, PDB-6rko:
Cryo-EM structure of the E. coli cytochrome bd-I oxidase at 2.68 A resolution
Method: EM (single particle) / Resolution: 2.68 Å

Chemicals

ChemComp-UQ8:
Ubiquinone-8

ChemComp-POV:
(2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate / phospholipid*YM / POPC

ChemComp-HDD:
CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE / Heme

ChemComp-HEB:
HEME B/C

ChemComp-OXY:
OXYGEN MOLECULE / Oxygen

ChemComp-HOH:
WATER / Water

Source
  • Escherichia coli K-12 (bacteria)
  • escherichia coli (strain k12) (bacteria)
KeywordsMEMBRANE PROTEIN / Oxidoreductase Cytochrome bd oxidase bd oxidase Oxidase

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