9ufw | pdb_00009ufw

Ubiquinol Binding Site of Cytochrome bo3 from Acinetobacter baumannii

spinqualitylabelsall models 9ufw, resolution 3.12Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9ufw is a 4 chain structure with sequence from Acinetobacter baumannii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.12Å Ligands: 3PE, CU, HEM, HEO, LMG, UQ8 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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(3) 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(3) 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. Structure of Acinetobacter baumannii cytochrome bo(3) ubiquinol oxidase.,Li Q, Hao R, Zhu J, Li J J Biol Chem. 2026 Apr;302(4):111324. doi: 10.1016/j.jbc.2026.111324. Epub 2026 , Feb 26. PMID:41759743 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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