8QC1
Respiratory complex I from Paracoccus denitrificans in MSP2N2 nanodiscs (ND4 & ND5 focus refinement)
Summary for 8QC1
| Entry DOI | 10.2210/pdb8qc1/pdb |
| EMDB information | 18325 |
| Descriptor | NADH dehydrogenase subunit M, NADH dehydrogenase subunit L, 1,2-DIACYL-GLYCEROL-3-SN-PHOSPHATE, ... (8 entities in total) |
| Functional Keywords | respiratory complex i, nadh:ubiquinone oxidoreductase, nanodiscs, oxidoreductase |
| Biological source | Paracoccus denitrificans PD1222 More |
| Total number of polymer chains | 2 |
| Total formula weight | 145259.70 |
| Authors | Ivanov, B.S.,Bridges, H.R.,Hirst, J. (deposition date: 2023-08-25, release date: 2024-09-11, Last modification date: 2025-03-26) |
| Primary citation | Ivanov, B.S.,Bridges, H.R.,Jarman, O.D.,Hirst, J. Structure of the turnover-ready state of an ancestral respiratory complex I. Nat Commun, 15:9340-9340, 2024 Cited by PubMed Abstract: Respiratory complex I is pivotal for cellular energy conversion, harnessing energy from NADH:ubiquinone oxidoreduction to drive protons across energy-transducing membranes for ATP synthesis. Despite detailed structural information on complex I, its mechanism of catalysis remains elusive due to lack of accompanying functional data for comprehensive structure-function analyses. Here, we present the 2.3-Å resolution structure of complex I from the α-proteobacterium Paracoccus denitrificans, a close relative of the mitochondrial progenitor, in phospholipid-bilayer nanodiscs. Three eukaryotic-type supernumerary subunits (NDUFS4, NDUFS6 and NDUFA12) plus a novel L-isoaspartyl-O-methyltransferase are bound to the core complex. Importantly, the enzyme is in a single, homogeneous resting state that matches the closed, turnover-ready (active) state of mammalian complex I. Our structure reveals the elements that stabilise the closed state and completes P. denitrificans complex I as a unified platform for combining structure, function and genetics in mechanistic studies. PubMed: 39472559DOI: 10.1038/s41467-024-53679-3 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.5 Å) |
Structure validation
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