6GCS
Cryo-EM structure of respiratory complex I from Yarrowia lipolytica
Summary for 6GCS
| Entry DOI | 10.2210/pdb6gcs/pdb |
| EMDB information | 4384 |
| Descriptor | 75-KDA PROTEIN (NUAM), NUJM SUBUNIT, PSST SUBUNIT (NUKM), ... (50 entities in total) |
| Functional Keywords | complex i, nadh dehydrogenase, mitochondrion proton pumping, ubiquinone, oxidoreductase |
| Biological source | Yarrowia lipolytica More |
| Total number of polymer chains | 42 |
| Total formula weight | 935297.12 |
| Authors | |
| Primary citation | Parey, K.,Brandt, U.,Xie, H.,Mills, D.J.,Siegmund, K.,Vonck, J.,Kuehlbrandt, W.,Zickermann, V. Cryo-EM structure of respiratory complex I at work. Elife, 7:-, 2018 Cited by PubMed Abstract: Mitochondrial complex I has a key role in cellular energy metabolism, generating a major portion of the proton motive force that drives aerobic ATP synthesis. The hydrophilic arm of the L-shaped ~1 MDa membrane protein complex transfers electrons from NADH to ubiquinone, providing the energy to drive proton pumping at distant sites in the membrane arm. The critical steps of energy conversion are associated with the redox chemistry of ubiquinone. We report the cryo-EM structure of complete mitochondrial complex I from the aerobic yeast both in the deactive form and after capturing the enzyme during steady-state activity. The site of ubiquinone binding observed during turnover supports a two-state stabilization change mechanism for complex I. PubMed: 30277212DOI: 10.7554/eLife.39213 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.32 Å) |
Structure validation
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