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-Structure paper
Title | Conformational changes in mitochondrial complex I of the thermophilic eukaryote . |
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Journal, issue, pages | Sci Adv, Vol. 8, Issue 47, Page eadc9952, Year 2022 |
Publish date | Nov 25, 2022 |
Authors | Eike Laube / Jakob Meier-Credo / Julian D Langer / Werner Kühlbrandt / |
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. ...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. |
External links | Sci Adv / PubMed:36427319 / PubMed Central |
Methods | EM (single particle) |
Resolution | 2.44 - 2.83 Å |
Structure data | EMDB-14791, PDB-7zm7: EMDB-14792, PDB-7zm8: EMDB-14794, PDB-7zmb: EMDB-14796, PDB-7zme: EMDB-14797, PDB-7zmg: EMDB-14798, PDB-7zmh: |
Chemicals | ChemComp-PC1: ChemComp-LMT: ChemComp-CDL: ChemComp-3PE: ChemComp-FES: ChemComp-SF4: ChemComp-FMN: ChemComp-NDP: ChemComp-ZN: ChemComp-ZMP: ChemComp-HOH: ChemComp-LMN: |
Source |
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Keywords | OXIDOREDUCTASE / Proton transporter / Mitochondrial membrane protein / Complex |