1BE3

CYTOCHROME BC1 COMPLEX FROM BOVINE

Summary for 1BE3

• Entry DOI: 10.2210/pdb1be3/pdb
• Descriptor: CYTOCHROME BC1 COMPLEX, PROTOPORPHYRIN IX CONTAINING FE, HEME C, ... (14 entities in total)
• Functional Keywords: electron transport, cytochrome, membrane protein
• Biological source: Bos taurus (cattle); More
• Cellular location: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side: P31800 P23004; Mitochondrion inner membrane: P00130 P07552 P13272 P00129 P13271 P00126 P13272; Mitochondrion inner membrane; Multi-pass membrane protein (By similarity): P00157; Mitochondrion inner membrane; Single-pass membrane protein; Intermembrane side: P00125
• Total number of polymer chains: 11
• Total formula weight: 243163.51

Authors

Iwata, S.,Lee, J.W.,Okada, K.,Lee, J.K.,Iwata, M.,Ramaswamy, S.,Jap, B.K. (deposition date: 1998-05-19, release date: 1999-01-13, Last modification date: 2024-10-16)

Primary citation

Iwata, S.,Lee, J.W.,Okada, K.,Lee, J.K.,Iwata, M.,Rasmussen, B.,Link, T.A.,Ramaswamy, S.,Jap, B.K.
Complete structure of the 11-subunit bovine mitochondrial cytochrome bc1 complex.
Science, 281:64-71, 1998

PubMed Abstract: Mitochondrial cytochrome bc1 complex performs two functions: It is a respiratory multienzyme complex and it recognizes a mitochondrial targeting presequence. Refined crystal structures of the 11-subunit bc1 complex from bovine heart reveal full views of this bifunctional enzyme. The "Rieske" iron-sulfur protein subunit shows significant conformational changes in different crystal forms, suggesting a new electron transport mechanism of the enzyme. The mitochondrial targeting presequence of the "Rieske" protein (subunit 9) is lodged between the two "core" subunits at the matrix side of the complex. These "core" subunits are related to the matrix processing peptidase, and the structure unveils how mitochondrial targeting presequences are recognized.

PubMed: 9651245
DOI: 10.1126/science.281.5373.64

Experimental method

X-RAY DIFFRACTION (3 Å)