1QCR

CRYSTAL STRUCTURE OF BOVINE MITOCHONDRIAL CYTOCHROME BC1 COMPLEX, ALPHA CARBON ATOMS ONLY

Summary for 1QCR

• Entry DOI: 10.2210/pdb1qcr/pdb
• Descriptor: UBIQUINOL CYTOCHROME C OXIDOREDUCTASE, PROTOPORPHYRIN IX CONTAINING FE, ... (12 entities in total)
• Functional Keywords: bc1, qcr, membrane protein, proton translocation, electron transfer, protease, mpp, mitochondrial processing peptidase, cytochrome c1, cytochrome b, rieske, iron sulfer protein, oxidoreductase
• Biological source: Bos taurus (cattle); More
• Cellular location: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side: P31800 P23004; Mitochondrion inner membrane: P00130 P07552 P00129 P13271 P00126; Mitochondrion inner membrane; Multi-pass membrane protein (By similarity): P00157; Mitochondrion inner membrane; Single-pass membrane protein; Intermembrane side: P00125; Mitochondrion inner membrane; Single-pass membrane protein: P13272 P13272
• Total number of polymer chains: 11
• Total formula weight: 210712.73

Authors

Xia, D.,Yu, C.A.,Kim, H.,Xia, J.Z.,Kachurin, A.,Zhang, L.,Yu, L.,Deisenhofer, J. (deposition date: 1997-05-17, release date: 1998-10-14, Last modification date: 2024-02-14)

Primary citation

Xia, D.,Yu, C.A.,Kim, H.,Xia, J.Z.,Kachurin, A.M.,Zhang, L.,Yu, L.,Deisenhofer, J.
Crystal structure of the cytochrome bc1 complex from bovine heart mitochondria.
Science, 277:60-66, 1997

PubMed Abstract: 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.

PubMed: 9204897
DOI: 10.1126/science.277.5322.60

Experimental method

X-RAY DIFFRACTION (2.7 Å)