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TitleCryo-EM structure of cytochrome bo quinol oxidase assembled in peptidiscs reveals an "open" conformation for potential ubiquinone-8 release.
Journal, issue, pagesBiochim Biophys Acta Bioenerg, Vol. 1865, Issue 3, Page 149045, Year 2024
Publish dateApr 11, 2024
AuthorsYe Gao / Yue Zhang / Sneha Hakke / Ronny Mohren / Lyanne J P M Sijbers / Peter J Peters / Raimond B G Ravelli /
PubMed AbstractCytochrome bo quinol oxidase belongs to the heme‑copper-oxidoreductase (HCO) superfamily, which is part of the respiratory chain and essential for cell survival. While the reaction mechanism of cyt ...Cytochrome bo quinol oxidase belongs to the heme‑copper-oxidoreductase (HCO) superfamily, which is part of the respiratory chain and essential for cell survival. While the reaction mechanism of cyt bo has been studied extensively over the last decades, specific details about its substrate binding and product release have remained unelucidated due to the lack of structural information. Here, we report a 2.8 Å cryo-electron microscopy structure of cyt bo from Escherichia coli assembled in peptidiscs. Our structural model shows a conformation for amino acids 1-41 of subunit I different from all previously published structures while the remaining parts of this enzyme are similar. Our new conformation shows a "U-shape" assembly in contrast to the transmembrane helix, named "TM0", in other reported structural models. However, TM0 blocks ubiquinone-8 (reaction product) release, suggesting that other cyt bo conformations should exist. Our structural model presents experimental evidence for an "open" conformation to facilitate substrate/product exchange. This work helps further understand the reaction cycle of this oxidase, which could be a benefit for potential drug/antibiotic design for health science.
External linksBiochim Biophys Acta Bioenerg / PubMed:38614453
MethodsEM (single particle)
Resolution2.8 Å
Structure data

18594

8qqk

EMDB-18594, PDB-8qqk:
Cryo-EM structure of E. coli cytochrome bo3 quinol oxidase assembled in peptidiscs
Method: EM (single particle) / Resolution: 2.8 Å

Chemicals

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

ChemComp-3PE:
1,2-Distearoyl-sn-glycerophosphoethanolamine / phospholipid*YM / Phosphatidylethanolamine

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE / Heme B

ChemComp-HEO:
HEME O / Heme O

ChemComp-CU:
COPPER (II) ION / Copper

Source
  • Escherichia coli (E. coli)
  • escherichia coli bl21(de3) (bacteria)
KeywordsMEMBRANE PROTEIN / E. coli / Ni-NTA resin / cytochrome bo3 quinol oxidase; ubiquinone-8 release; peptidisc; single particle analysis; cryo-EM

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