7ZMG
CryoEM structure of mitochondrial complex I from Chaetomium thermophilum (state 1)
Summary for 7ZMG
| Entry DOI | 10.2210/pdb7zmg/pdb |
| Related | 7ZM7 7ZM8 7ZMB 7ZME 7ZMH |
| EMDB information | 14797 |
| Descriptor | NADH-ubiquinone oxidoreductase chain 1, NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial, NADH-ubiquinone oxidoreductase 49 kDa subunit-like protein, ... (53 entities in total) |
| Functional Keywords | proton transporter, mitochondrial membrane protein, complex, oxidoreductase |
| Biological source | Chaetomium thermophilum var. thermophilum DSM 1495 More |
| Total number of polymer chains | 43 |
| Total formula weight | 1219033.60 |
| Authors | Laube, E.,Kuehlbrandt, W. (deposition date: 2022-04-19, release date: 2022-11-30, Last modification date: 2024-10-23) |
| Primary citation | Laube, E.,Meier-Credo, J.,Langer, J.D.,Kuhlbrandt, W. Conformational changes in mitochondrial complex I of the thermophilic eukaryote Chaetomium thermophilum. Sci Adv, 8:eadc9952-eadc9952, 2022 Cited by PubMed Abstract: Mitochondrial complex I is a redox-driven proton pump that generates proton-motive force across the inner mitochondrial membrane, powering oxidative phosphorylation and ATP synthesis in eukaryotes. We report the structure of complex I from the thermophilic fungus , determined by cryoEM up to 2.4-Å resolution. We show that the complex undergoes a transition between two conformations, which we refer to as state 1 and state 2. The conformational switch is manifest in a twisting movement of the peripheral arm relative to the membrane arm, but most notably in substantial rearrangements of the Q-binding cavity and the E-channel, resulting in a continuous aqueous passage from the E-channel to subunit ND5 at the far end of the membrane arm. The conformational changes in the complex interior resemble those reported for mammalian complex I, suggesting a highly conserved, universal mechanism of coupling electron transport to proton pumping. PubMed: 36427319DOI: 10.1126/sciadv.adc9952 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.44 Å) |
Structure validation
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