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-Structure paper
Title | Mitochondrial complex I structure reveals ordered water molecules for catalysis and proton translocation. |
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Journal, issue, pages | Nat Struct Mol Biol, Vol. 27, Issue 10, Page 892-900, Year 2020 |
Publish date | Aug 3, 2020 |
Authors | Daniel N Grba / Judy Hirst / |
PubMed Abstract | Mitochondrial complex I powers ATP synthesis by oxidative phosphorylation, exploiting the energy from ubiquinone reduction by NADH to drive protons across the energy-transducing inner membrane. ...Mitochondrial complex I powers ATP synthesis by oxidative phosphorylation, exploiting the energy from ubiquinone reduction by NADH to drive protons across the energy-transducing inner membrane. Recent cryo-EM analyses of mammalian and yeast complex I have revolutionized structural and mechanistic knowledge and defined structures in different functional states. Here, we describe a 2.7-Å-resolution structure of the 42-subunit complex I from the yeast Yarrowia lipolytica containing 275 structured water molecules. We identify a proton-relay pathway for ubiquinone reduction and water molecules that connect mechanistically crucial elements and constitute proton-translocation pathways through the membrane. By comparison with known structures, we deconvolute structural changes governing the mammalian 'deactive transition' (relevant to ischemia-reperfusion injury) and their effects on the ubiquinone-binding site and a connected cavity in ND1. Our structure thus provides important insights into catalysis by this enigmatic respiratory machine. |
External links | Nat Struct Mol Biol / PubMed:32747785 / PubMed Central |
Methods | EM (single particle) |
Resolution | 2.7 Å |
Structure data | EMDB-10815, PDB-6yj4: |
Chemicals | ChemComp-3PE: ChemComp-SF4: ChemComp-LMT: ChemComp-PLC: ChemComp-FES: ChemComp-FMN: ChemComp-CDL: ChemComp-NDP: ChemComp-ZN: ChemComp-EHZ: ChemComp-HOH: |
Source |
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Keywords | MEMBRANE PROTEIN / NADH:Ubiquinone Oxidoreductase / complex I |