8BA0
Drosophila melanogaster complex I in the Twisted state (Dm2)
Summary for 8BA0
| Entry DOI | 10.2210/pdb8ba0/pdb |
| EMDB information | 15937 |
| Descriptor | NADH-ubiquinone oxidoreductase chain 3, NADH-ubiquinone oxidoreductase chain 6, NADH-ubiquinone oxidoreductase chain 4L, ... (51 entities in total) |
| Functional Keywords | mitochondrial complex i, respiratory complex i, nadh:ubiquinone oxidoreductase, ubiquinone, oxidoreductase |
| Biological source | Drosophila melanogaster (fruit fly) More |
| Total number of polymer chains | 43 |
| Total formula weight | 965756.30 |
| Authors | Agip, A.N.A.,Chung, I.,Sanchez-Martinez, A.,Whitworth, A.J.,Hirst, J. (deposition date: 2022-10-10, release date: 2023-01-18, Last modification date: 2024-10-09) |
| Primary citation | Agip, A.A.,Chung, I.,Sanchez-Martinez, A.,Whitworth, A.J.,Hirst, J. Cryo-EM structures of mitochondrial respiratory complex I from Drosophila melanogaster. Elife, 12:-, 2023 Cited by PubMed Abstract: Respiratory complex I powers ATP synthesis by oxidative phosphorylation, exploiting the energy from NADH oxidation by ubiquinone to drive protons across an energy-transducing membrane. is a candidate model organism for complex I due to its high evolutionary conservation with the mammalian enzyme, well-developed genetic toolkit, and complex physiology for studies in specific cell types and tissues. Here, we isolate complex I from and determine its structure, revealing a 43-subunit assembly with high structural homology to its 45-subunit mammalian counterpart, including a hitherto unknown homologue to subunit NDUFA3. The major conformational state of the enzyme is the mammalian-type 'ready-to-go' active resting state, with a fully ordered and enclosed ubiquinone-binding site, but a subtly altered global conformation related to changes in subunit ND6. The mammalian-type 'deactive' pronounced resting state is not observed: in two minor states, the ubiquinone-binding site is unchanged, but a deactive-type π-bulge is present in ND6-TMH3. Our detailed structural knowledge of complex I provides a foundation for new approaches to disentangle mechanisms of complex I catalysis and regulation in bioenergetics and physiology. PubMed: 36622099DOI: 10.7554/eLife.84424 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.68 Å) |
Structure validation
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