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Structure paper

TitleStructure of Acinetobacter baumannii cytochrome bo ubiquinol oxidase.
Journal, issue, pagesJ Biol Chem, Vol. 302, Issue 4, Page 111324, Year 2026
Publish dateFeb 26, 2026
AuthorsQuan Li / Rui Hao / Jiapeng Zhu / Jiao Li /
PubMed AbstractHeme-copper oxidases (heme-copper oxidoreductases) are terminal oxidases that couple oxygen reduction to proton pumping for ATP synthesis. Although our previous work has elucidated the structure and ...Heme-copper oxidases (heme-copper oxidoreductases) are terminal oxidases that couple oxygen reduction to proton pumping for ATP synthesis. Although our previous work has elucidated the structure and proton transfer mechanism of the Escherichia coli cytochrome bo ubiquinol oxidase, the quinone dynamics and structural diversity across heme-copper oxidoreductases remain unclear. Here, we report the high-resolution cryo-EM structures of cytochrome bo ubiquinol oxidase from the pathogen Acinetobacter baumannii. We captured four distinct conformational states of its native ubiquinone-8 substrate within the binding pocket. Comparative analysis revealed that conformational transitions of the substrate are directly coupled to movements of the transmembrane 0 helix. Notably, in the locked state, the substrate headgroup is stabilized by specific hydrogen bonds and adopts a distinct depth and orientation. In addition, a unique hairpin-like loop was identified in subunit II, a specific feature absent in the homologs. Our observations not only provide structural details of a pathogenic respiratory terminal oxidase but also reveal a dynamic substrate catalytic mechanism, highlighting potential avenues for targeting bacterial energy metabolism.
External linksJ Biol Chem / PubMed:41759743 / PubMed Central
MethodsEM (single particle)
Resolution3.05 - 3.56 Å
Structure data

64104

9ufb

EMDB-64104, PDB-9ufb:
Ubiquinol Binding Site of Cytochrome bo3 from A.b
Method: EM (single particle) / Resolution: 3.05 Å

64122

9uft

EMDB-64122, PDB-9uft:
Ubiquinol Binding Site of Cytochrome bo3 from Acinetobacter baumannii
Method: EM (single particle) / Resolution: 3.56 Å

64123

9ufv

EMDB-64123, PDB-9ufv:
Ubiquinol Binding Site of Cytochrome bo3 from Acinetobacter baumannii
Method: EM (single particle) / Resolution: 3.56 Å

64124

9ufw

EMDB-64124, PDB-9ufw:
Ubiquinol Binding Site of Cytochrome bo3 from Acinetobacter baumannii
Method: EM (single particle) / Resolution: 3.12 Å

64127

9ufz

EMDB-64127, PDB-9ufz:
Ubiquinol Binding Site of Cytochrome bo3 from Acinetobacter baumannii
Method: EM (single particle) / Resolution: 3.28 Å

Chemicals

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

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

ChemComp-HEO:
HEME O

ChemComp-CU:
COPPER (II) ION

ChemComp-UQ8:
Ubiquinone-8

ChemComp-LMG:
1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE

Source
  • acinetobacter baumannii (bacteria)
KeywordsOXIDOREDUCTASE / protein pump / ubiquinol / oxidase

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