1qcr
CRYSTAL STRUCTURE OF BOVINE MITOCHONDRIAL CYTOCHROME BC1 COMPLEX, ALPHA CARBON ATOMS ONLY
|
OverviewOverview
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 bc1, complex were built, including core 1, core 2, cytochrome b, subunit 6, subunit 7, a carboxyl-terminal fragment of cytochrome c1, and an, amino-terminal fragment of the iron-sulfur protein. The positions of the, four iron centers within the bc1 complex and the binding sites of the two, specific respiratory inhibitors antimycin A and myxothiazol were, identified. The membrane-spanning region of each bc1 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.
About this StructureAbout this Structure
1QCR is a Protein complex structure of sequences from Bos taurus with HEM as ligand. Active as Ubiquinol--cytochrome-c reductase, with EC number 1.10.2.2 Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the cytochrome bc1 complex from bovine heart mitochondria., Xia D, Yu CA, Kim H, Xia JZ, Kachurin AM, Zhang L, Yu L, Deisenhofer J, Science. 1997 Jul 4;277(5322):60-6. PMID:9204897
Page seeded by OCA on Wed Nov 21 00:34:42 2007