2YBB

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

Summary for 2YBB

• Entry DOI: 10.2210/pdb2ybb/pdb
• EMDB information: 1876
• Descriptor: NADH-QUINONE OXIDOREDUCTASE SUBUNIT 1, CYTOCHROME B-C1 COMPLEX SUBUNIT 2, MITOCHONDRIAL, CYTOCHROME B, ... (52 entities in total)
• Functional Keywords: supercomplex b, mitochondria, respiratory chain, oxidoreductase, amphipol a8-35, random conical tilt
• Biological source: THERMUS THERMOPHILUS; More
• Total number of polymer chains: 48
• Total formula weight: 1125224.33

Authors

Althoff, T.,Mills, D.J.,Popot, J.-L.,Kuehlbrandt, W. (deposition date: 2011-03-02, release date: 2011-10-19, Last modification date: 2024-11-20)

Primary citation

Althoff, T.,Mills, D.J.,Popot, J.-L.,Kuehlbrandt, W.
Arrangement of Electron Transport Chain Components in Bovine Mitochondrial Supercomplex I(1)III(2)Iv(1).
Embo J., 30:4652-, 2011

PubMed Abstract: 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-Å 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.

PubMed: 21909073
DOI: 10.1038/EMBOJ.2011.324

Experimental method

ELECTRON MICROSCOPY (19 Å)