4UQ8
Electron cryo-microscopy of bovine Complex I
Summary for 4UQ8
| Entry DOI | 10.2210/pdb4uq8/pdb |
| EMDB information | 2676 |
| Descriptor | NADH UBIQUINONE OXIDOREDUCTASE CHAIN 3, NADH UBIQUINONE OXIDOREDUCTASE CHAIN 6, NADH UBIQUINONE OXIDOREDUCTASE CHAIN 4L, ... (45 entities in total) |
| Functional Keywords | nadh dehydrogenase, respiratory complex, oxidoreductase |
| Biological source | BOS TAURUS (CATTLE) More |
| Total number of polymer chains | 49 |
| Total formula weight | 517635.08 |
| Authors | Vinothkumar, K.R.,Zhu, J.,Hirst, J. (deposition date: 2014-06-21, release date: 2014-10-01, Last modification date: 2024-05-08) |
| Primary citation | Vinothkumar, K.R.,Zhu, J.,Hirst, J. Architecture of Mammalian Respiratory Complex I. Nature, 515:80-, 2014 Cited by PubMed Abstract: Complex I (NADH:ubiquinone oxidoreductase) is essential for oxidative phosphorylation in mammalian mitochondria. It couples electron transfer from NADH to ubiquinone with proton translocation across the energy-transducing inner membrane, providing electrons for respiration and driving ATP synthesis. Mammalian complex I contains 44 different nuclear- and mitochondrial-encoded subunits, with a combined mass of 1 MDa. The 14 conserved 'core' subunits have been structurally defined in the minimal, bacterial complex, but the structures and arrangement of the 30 'supernumerary' subunits are unknown. Here we describe a 5 Å resolution structure of complex I from Bos taurus heart mitochondria, a close relative of the human enzyme, determined by single-particle electron cryo-microscopy. We present the structures of the mammalian core subunits that contain eight iron-sulphur clusters and 60 transmembrane helices, identify 18 supernumerary transmembrane helices, and assign and model 14 supernumerary subunits. Thus, we considerably advance knowledge of the structure of mammalian complex I and the architecture of its supernumerary ensemble around the core domains. Our structure provides insights into the roles of the supernumerary subunits in regulation, assembly and homeostasis, and a basis for understanding the effects of mutations that cause a diverse range of human diseases. PubMed: 25209663DOI: 10.1038/NATURE13686 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.95 Å) |
Structure validation
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