Three-dimensional structure of bovine cytochrome bc1 complex by electron cryomicroscopy and helical image reconstruction

Cytochrome bc1 complex from bovine heart has been reconstituted into tubular crystals. The three-dimensional structure of the complex in lipid bilayer has been obtained at an effective resolution of 16 angstrom by electron cryomicroscopy and helical image reconstruction. The complex is in a dimeric...

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Published inNature structural biology Vol. 3; no. 6; p. 553
Main Authors Akiba, T, Toyoshima, C, Matsunaga, T, Kawamoto, M, Kubota, T, Fukuyama, K, Namba, K, Matsubara, H
Format Journal Article
LanguageEnglish
Published United States 01.06.1996
Subjects
Animals
Binding Sites
Cattle
Cell Membrane - chemistry
Cell Membrane - metabolism
Cell Membrane - ultrastructure
Computer Simulation
Crystallization
Electron Transport Complex III - chemistry
Electron Transport Complex III - metabolism
Electron Transport Complex III - ultrastructure
Freezing
Lipid Bilayers
Microscopy, Electron
Models, Molecular
Neurospora - enzymology
Oxidation-Reduction
Ubiquinone - metabolism
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Summary:Cytochrome bc1 complex from bovine heart has been reconstituted into tubular crystals. The three-dimensional structure of the complex in lipid bilayer has been obtained at an effective resolution of 16 angstrom by electron cryomicroscopy and helical image reconstruction. The complex is in a dimeric form, in which the monomers are associated closely in extramembrane domains on both sides of the membrane. The large inner domain is distinctively hollow and the small outer domain consists of a flat mass and two bulbous extrusions. These domains are connected by two narrow transmembrane columns. Locations of the subunits and the redox centres in the model are proposed.
ISSN:1072-8368
DOI:10.1038/nsb0696-553