2ybb | pdb_00002ybb

Fitted model for bovine mitochondrial supercomplex I1III2IV1 by single particle cryo-EM (EMD-1876)

spinqualitylabelsall models 2ybb, resolution 19.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2ybb is a 48 chain structure with sequence from Bos taurus, Escherichia coli and Thermus thermophilus. Full crystallographic information is available from OCA. Ligands: CA, CDL, CU, FES, FMN, HEA, HEC, HEM, MG, NAI, SF4, SMA, UQ1, ZN NonStd Res: UNK Activity: Glucokinase, with EC number 2.7.1.2 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed The respiratory chain in the inner mitochondrial membrane contains three large multi-enzyme complexes that together establish the proton gradient for ATP synthesis, and assemble into a supercomplex. A 19-A 3D map of the 1.7-MDa amphipol-solubilized supercomplex I(1)III(2)IV(1) from bovine heart obtained by single-particle electron cryo-microscopy reveals an amphipol belt replacing the membrane lipid bilayer. A precise fit of the X-ray structures of complex I, the complex III dimer, and monomeric complex IV indicates distances of 13 nm between the ubiquinol-binding sites of complexes I and III, and of 10-11 nm between the cytochrome c binding sites of complexes III and IV. The arrangement of respiratory chain complexes suggests two possible pathways for efficient electron transfer through the supercomplex, of which the shorter branch through the complex III monomer proximal to complex I may be preferred. Arrangement of electron transport chain components in bovine mitochondrial supercomplex I(1)III(2)IV(1).,Althoff T, Mills DJ, Popot JL, Kuhlbrandt W EMBO J. 2011 Sep 9. doi: 10.1038/emboj.2011.324. PMID:21909073 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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