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7O71

Cryo-EM structure of a respiratory complex I

Summary for 7O71
Entry DOI10.2210/pdb7o71/pdb
EMDB information12742
DescriptorNADH-ubiquinone oxidoreductase 78 kDa subunit, Subunit NB5M of NADH:Ubiquinone Oxidoreductase (Complex I), NADH-ubiquinone oxidoreductase chain 1, ... (55 entities in total)
Functional Keywordscomplex i, nadh dehydrogenase, mitochondrion proton pumping, ubiquinone, oxidoreductase
Biological sourceYarrowia lipolytica (Candida lipolytica)
More
Total number of polymer chains42
Total formula weight1015124.29
Authors
Parey, K.,Vonck, J. (deposition date: 2021-04-12, release date: 2021-11-10, Last modification date: 2025-10-01)
Primary citationParey, K.,Lasham, J.,Mills, D.J.,Djurabekova, A.,Haapanen, O.,Yoga, E.G.,Xie, H.,Kuhlbrandt, W.,Sharma, V.,Vonck, J.,Zickermann, V.
High-resolution structure and dynamics of mitochondrial complex I-Insights into the proton pumping mechanism.
Sci Adv, 7:eabj3221-eabj3221, 2021
Cited by
PubMed Abstract: Mitochondrial NADH:ubiquinone oxidoreductase (complex I) is a 1-MDa membrane protein complex with a central role in energy metabolism. Redox-driven proton translocation by complex I contributes substantially to the proton motive force that drives ATP synthase. Several structures of complex I from bacteria and mitochondria have been determined, but its catalytic mechanism has remained controversial. We here present the cryo-EM structure of complex I from at 2.1-Å resolution, which reveals the positions of more than 1600 protein-bound water molecules, of which ~100 are located in putative proton translocation pathways. Another structure of the same complex under steady-state activity conditions at 3.4-Å resolution indicates conformational transitions that we associate with proton injection into the central hydrophilic axis. By combining high-resolution structural data with site-directed mutagenesis and large-scale molecular dynamic simulations, we define details of the proton translocation pathways and offer insights into the redox-coupled proton pumping mechanism of complex I.
PubMed: 34767441
DOI: 10.1126/sciadv.abj3221
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.4 Å)
Structure validation

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