6ZKA
Membrane domain of open complex I during turnover
Summary for 6ZKA
| Entry DOI | 10.2210/pdb6zka/pdb |
| EMDB information | 11242 |
| Descriptor | NADH-ubiquinone oxidoreductase chain 3, Acyl carrier protein, NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8, ... (37 entities in total) |
| Functional Keywords | complex, respiration, nadh, proton pump, mitochondria, iron-sulphur cluster, oxidoreductase, membrane protein, electron transport |
| Biological source | Ovis aries (Sheep) More |
| Total number of polymer chains | 29 |
| Total formula weight | 660272.69 |
| Authors | Kampjut, D.,Sazanov, L.A. (deposition date: 2020-06-30, release date: 2020-10-07, Last modification date: 2025-04-09) |
| Primary citation | Kampjut, D.,Sazanov, L.A. The coupling mechanism of mammalian respiratory complex I. Science, 370:-, 2020 Cited by PubMed Abstract: Mitochondrial complex I couples NADH:ubiquinone oxidoreduction to proton pumping by an unknown mechanism. Here, we present cryo-electron microscopy structures of ovine complex I in five different conditions, including turnover, at resolutions up to 2.3 to 2.5 angstroms. Resolved water molecules allowed us to experimentally define the proton translocation pathways. Quinone binds at three positions along the quinone cavity, as does the inhibitor rotenone that also binds within subunit ND4. Dramatic conformational changes around the quinone cavity couple the redox reaction to proton translocation during open-to-closed state transitions of the enzyme. In the induced deactive state, the open conformation is arrested by the ND6 subunit. We propose a detailed molecular coupling mechanism of complex I, which is an unexpected combination of conformational changes and electrostatic interactions. PubMed: 32972993DOI: 10.1126/science.abc4209 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.5 Å) |
Structure validation
Download full validation report
