6yj4 | pdb_00006yj4

Structure of Yarrowia lipolytica complex I at 2.7 A

spinqualitylabelsall models 6yj4, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6yj4 is a 10 chain structure with sequence from Yarrowia lipolytica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 2.7Å Ligands: 2MR, 3PE, CDL, EHZ, FES, FME, FMN, LMT, NDP, PLC, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q6C674_YARLI Publication Abstract from PubMed 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-A-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. Mitochondrial complex I structure reveals ordered water molecules for catalysis and proton translocation.,Grba DN, Hirst J Nat Struct Mol Biol. 2020 Aug 3. pii: 10.1038/s41594-020-0473-x. doi:, 10.1038/s41594-020-0473-x. PMID:32747785 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA