7DEG
Cryo-EM structure of a heme-copper terminal oxidase dimer provides insights into its catalytic mechanism
Summary for 7DEG
| Entry DOI | 10.2210/pdb7deg/pdb |
| EMDB information | 30657 |
| Descriptor | Cytochrome c oxidase subunit I, DINUCLEAR COPPER ION, Cytochrome oxidase subunit IIa, ... (10 entities in total) |
| Functional Keywords | electron cryo-microscopy, heme-copper oxidase, cytochrome c oxidase dimer, aquifex aeolicus, naphthoquinone, oxidoreductase |
| Biological source | Aquifex aeolicus (strain VF5) More |
| Total number of polymer chains | 6 |
| Total formula weight | 183295.85 |
| Authors | Fei, S.,Hartmut, M.,Yun, Z.,Guoliang, Z.,Shuangbo, Z. (deposition date: 2020-11-04, release date: 2021-08-04, Last modification date: 2025-04-09) |
| Primary citation | Zhu, G.,Zeng, H.,Zhang, S.,Juli, J.,Tai, L.,Zhang, D.,Pang, X.,Zhang, Y.,Lam, S.M.,Zhu, Y.,Peng, G.,Michel, H.,Sun, F. The Unusual Homodimer of a Heme-Copper Terminal Oxidase Allows Itself to Utilize Two Electron Donors. Angew.Chem.Int.Ed.Engl., 60:13323-13330, 2021 Cited by PubMed Abstract: The heme-copper oxidase superfamily comprises cytochrome c and ubiquinol oxidases. These enzymes catalyze the transfer of electrons from different electron donors onto molecular oxygen. A B-family cytochrome c oxidase from the hyperthermophilic bacterium Aquifex aeolicus was discovered previously to be able to use both cytochrome c and naphthoquinol as electron donors. Its molecular mechanism as well as the evolutionary significance are yet unknown. Here we solved its 3.4 Å resolution electron cryo-microscopic structure and discovered a novel dimeric structure mediated by subunit I (CoxA2) that would be essential for naphthoquinol binding and oxidation. The unique structural features in both proton and oxygen pathways suggest an evolutionary adaptation of this oxidase to its hyperthermophilic environment. Our results add a new conceptual understanding of structural variation of cytochrome c oxidases in different species. PubMed: 33665933DOI: 10.1002/anie.202016785 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.4 Å) |
Structure validation
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