7QHO
Cytochrome bcc-aa3 supercomplex (respiratory supercomplex III2/IV2) from Corynebacterium glutamicum (as isolated)
Summary for 7QHO
| Entry DOI | 10.2210/pdb7qho/pdb |
| EMDB information | 13977 |
| Descriptor | Cytochrome bc1 complex Rieske iron-sulfur subunit, Hypothetical membrane protein, Actinobacterial supercomplex, subunit C (AscC), ... (33 entities in total) |
| Functional Keywords | supercomplex, respiratory chain, cytochrome bcc-aa3 supercomplex, proton translocation, bioenergetics, membrane protein, electron transport, oxidoreductase |
| Biological source | Corynebacterium glutamicum ATCC 13032 More |
| Total number of polymer chains | 26 |
| Total formula weight | 767911.96 |
| Authors | Kao, W.-C.,Hunte, C. (deposition date: 2021-12-13, release date: 2022-05-18, Last modification date: 2024-10-23) |
| Primary citation | Kao, W.-C.,Ortmann de Percin Northumberland, C.,Cheng, T.C.,Ortiz, J.,Durand, A.,von Loeffelholz, O.,Schilling, O.,Biniossek, M.L.,Klaholz, B.P.,Hunte, C. Structural basis for safe and efficient energy conversion in a respiratory supercomplex Nature Communications, 13:545-, 2022 Cited by PubMed Abstract: Proton-translocating respiratory complexes assemble into supercomplexes that are proposed to increase the efficiency of energy conversion and limit the production of harmful reactive oxygen species during aerobic cellular respiration. Cytochrome bc complexes and cytochrome aa oxidases are major drivers of the proton motive force that fuels ATP generation via respiration, but how wasteful electron- and proton transfer is controlled to enhance safety and efficiency in the context of supercomplexes is not known. Here, we address this question with the 2.8 Å resolution cryo-EM structure of the cytochrome bcc-aa (III-IV) supercomplex from the actinobacterium Corynebacterium glutamicum. Menaquinone, substrate mimics, lycopene, an unexpected Q site, dioxygen, proton transfer routes, and conformational states of key protonable residues are resolved. Our results show how safe and efficient energy conversion is achieved in a respiratory supercomplex through controlled electron and proton transfer. The structure may guide the rational design of drugs against actinobacteria that cause diphtheria and tuberculosis. PubMed: 35087070DOI: 10.1038/s41467-022-28179-x PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.1 Å) |
Structure validation
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