6YJ4

Structure of Yarrowia lipolytica complex I at 2.7 A

Summary for 6YJ4

• Entry DOI: 10.2210/pdb6yj4/pdb
• EMDB information: 10815
• Descriptor: NADH-ubiquinone oxidoreductase chain 3, NADH-ubiquinone oxidoreductase chain 6, NADH-ubiquinone oxidoreductase chain 4L, ... (53 entities in total)
• Functional Keywords: nadh:ubiquinone oxidoreductase, complex i, membrane protein
• Biological source: Yarrowia lipolytica; More
• Total number of polymer chains: 42
• Total formula weight: 1020034.64

Authors

Hirst, J.,Grba, D. (deposition date: 2020-04-02, release date: 2020-08-12, Last modification date: 2025-04-09)

Primary citation

Grba, D.N.,Hirst, J.
Mitochondrial complex I structure reveals ordered water molecules for catalysis and proton translocation.
Nat.Struct.Mol.Biol., 27:892-900, 2020

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. 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.

PubMed: 32747785
DOI: 10.1038/s41594-020-0473-x

Experimental method

ELECTRON MICROSCOPY (2.7 Å)