Inhibitor-complexed Structures of the Cytochrome bc1 from the Photosynthetic Bacterium Rhodobacter sphaeroides

The cytochrome bc1 complex (bc1) is a major contributor to the proton motive force across the membrane by coupling electron transfer to proton translocation. The crystal structures of wild type and mutant bc1 complexes from the photosynthetic purple bacterium Rhodobacter sphaeroides (Rsbc1), stabili...

Full description

Saved in:
Bibliographic Details
Published in:The Journal of biological chemistry 2008-02, Vol.283 (5), p.2846-2857
Main Authors: Esser, Lothar, Elberry, Maria, Zhou, Fei, Yu, Chang-An, Yu, Linda, Xia, Di
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Antimycin A - analogs & derivatives
Antimycin A - pharmacology
Bacterial Proteins - antagonists & inhibitors
Bacterial Proteins - chemistry
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
Binding Sites
Crystallography, X-Ray
Electron Transport Complex III - antagonists & inhibitors
Electron Transport Complex III - chemistry
Electron Transport Complex III - genetics
Electron Transport Complex III - metabolism
Iron-Sulfur Proteins - chemistry
Models, Molecular
Molecular Sequence Data
Multiprotein Complexes
Mutagenesis, Site-Directed
Polyenes - pharmacology
Protein Subunits
Proton-Motive Force
Rhodobacter sphaeroides - chemistry
Rhodobacter sphaeroides - genetics
Rhodobacter sphaeroides - metabolism
Sequence Homology, Amino Acid
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The cytochrome bc1 complex (bc1) is a major contributor to the proton motive force across the membrane by coupling electron transfer to proton translocation. The crystal structures of wild type and mutant bc1 complexes from the photosynthetic purple bacterium Rhodobacter sphaeroides (Rsbc1), stabilized with the quinol oxidation (QP) site inhibitor stigmatellin alone or in combination with the quinone reduction (QN) site inhibitor antimycin, were determined. The high quality electron density permitted assignments of a new metal-binding site to the cytochrome c1 subunit and a number of lipid and detergent molecules. Structural differences between Rsbc1 and its mitochondrial counterparts are mostly extra membranous and provide a basis for understanding the function of the predominantly longer sequences in the bacterial subunits. Functional implications for the bc1 complex are derived from analyses of 10 independent molecules in various crystal forms and from comparisons with mitochondrial complexes.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M708608200