Nature Structural Biology
3, 553 - 561 (1996)
doi:10.1038/nsb0696-553
Three-dimensional structure of bovine cytochrome bC1 complex by electron cryomicroscopy and helical image reconstructionToshihiko Akiba1, Chikashi Toyoshima2, Takateru Matsunaga3, Masahide Kawamoto3, Tomomi Kubota4, Keiichi Fukuyama3, Keiichi Namba1
& Hiroshi Matsubara5
11nternational Institute for Advanced Research, Matsushita Electric Industrial Co., Ltd., 3−4 Hikaridai, Seika, Kyoto 619-02, Japan
2Institute of Molecular and Cellular Biosciences, The University of Tokyo, Bunkyo-ku, Tokyo 113, Japan
3Department of Biology, Faculty of Science, Osaka University, Toyonaka, Osaka 560, Japan
4National Institute of Biosdence and Human-Technology, Tsukuba, Ibaraki 305, Japan
5Department of Biochemistry, Faculty of Science, Okayama University of Science, Okayama, Okayama 700, Japan Cytochrome bc
1 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 Å 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. REFERENCES
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