9UFV
Ubiquinol Binding Site of Cytochrome bo3 from Acinetobacter baumannii
Summary for 9UFV
| Entry DOI | 10.2210/pdb9ufv/pdb |
| EMDB information | 64123 |
| Descriptor | Cytochrome bo(3) ubiquinol oxidase subunit 1, Ubiquinone-8, Ubiquinol oxidase subunit 2, ... (10 entities in total) |
| Functional Keywords | protein pump, ubiquinol, oxidase, oxidoreductase |
| Biological source | Acinetobacter baumannii More |
| Total number of polymer chains | 4 |
| Total formula weight | 146869.03 |
| Authors | |
| Primary citation | Li, Q.,Hao, R.,Zhu, J.,Li, J. Structure of Acinetobacter baumannii cytochrome bo 3 ubiquinol oxidase. J.Biol.Chem., 302:111324-111324, 2026 Cited by PubMed Abstract: 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. PubMed: 41759743DOI: 10.1016/j.jbc.2026.111324 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.56 Å) |
Structure validation
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