Crystal structure of the cytochrome bc{sub 1} complex from bovine heart mitochondria
- Univ. of Texas Southwestern Medical Center, Dallas, TX (United States)
- Oklahoma State Univ., Stillwater, OK (United States); and others
On the basis of x-ray diffraction data to a resolution of 2.9 angstroms, atomic models of most protein components of the bovine cytochrome bc{sub 1} complex were built, including core 1, core 2, cytochrome b, subunit 6, and subunit 7, a carboxyl-terminal fragment of cytochrome c{sub 1}, and an amino-terminal fragment of the iron-sulfur protein. The positions of the four iron centers within the bc{sub 1} complex and the binding sites of the two specific respiratory inhibitors antimycin A and myxothiazol were identified. The membrane-spanning region of each bc{sub 1} complex monomer consists of 13 transmembrane helices, eight of which belong to cytochrome b. Closely interacting monomers are arranged as symmetric dimers and form cavities through which the inhibitor binding pockets can be accessed. The proteins core 1 and core 2 are structurally similar to each other and consist of two domains of roughly equal size and identical folding topology. 39 refs., 5 figs., 2 tabs.
- OSTI ID:
- 569305
- Journal Information:
- Science, Vol. 277, Issue 5322; Other Information: PBD: 4 Jul 1997
- Country of Publication:
- United States
- Language:
- English
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