6zk9 | pdb_00006zk9

Peripheral domain of open complex I during turnover

spinqualitylabelsall models 6zk9, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6zk9 is a 10 chain structure with sequence from Ovis aries. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 2.3Å Ligands: 2MR, 3PE, AYA, CDL, FES, FMN, K, NAI, NDP, PC1, ZMP, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function W5PUX0_SHEEP Publication Abstract from PubMed Mitochondrial complex I couples NADH:ubiquinone oxidoreduction to proton pumping by an unknown mechanism. Here we present cryo-EM structures of ovine complex I in five different conditions, including turnover, at resolutions up to 2.3-2.5 A. Resolved water molecules allowed us to experimentally define the proton translocation pathways. Quinone binds at three positions along the quinone cavity, as does the inhibitor rotenone that also binds within subunit ND4. Dramatic conformational changes around the quinone cavity couple the redox reaction to proton translocation during "open" to "closed" state transitions of the enzyme. In the induced deactive state, the "open" conformation is arrested by the ND6 subunit. We propose a detailed molecular coupling mechanism of complex I, which is an unexpected combination of conformational changes and electrostatic interactions. The coupling mechanism of mammalian respiratory complex I.,Kampjut D, Sazanov LA Science. 2020 Sep 24. pii: science.abc4209. doi: 10.1126/science.abc4209. PMID:32972993 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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