1ZRT

Rhodobacter capsulatus cytochrome bc1 complex with stigmatellin bound

Summary for 1ZRT

• Entry DOI: 10.2210/pdb1zrt/pdb
• Related: 1KB9 1PP9 2qjy 2yiu 6XI0
• Descriptor: Cytochrome b, Cytochrome c1, Ubiquinol-cytochrome c reductase iron-sulfur subunit, ... (9 entities in total)
• Functional Keywords: cytochrome bc1, membrane protein, heme protein, rieske iron sulfur protein, cytochrome b, cytochrome c1, complex iii, oxidoreductase, redox enzyme, respiratory chain, stigmatellin, electron transport
• Biological source: Rhodobacter capsulatus; More
• Cellular location: Cell membrane; Multi-pass membrane protein (Potential): D5ANZ3; Cell membrane; Single-pass membrane protein (Potential): D5ANZ4; Cell membrane; Single-pass membrane protein: D5ANZ2
• Total number of polymer chains: 6
• Total formula weight: 202108.10

Authors

Berry, E.A.,Huang, L.S.,Saechao, L.K.,Pon, N.G.,Valkova-Valchanov, M.,Daldal, F. (deposition date: 2005-05-22, release date: 2005-06-07, Last modification date: 2024-11-20)

Primary citation

Berry, E.A.,Huang, L.S.,Saechao, L.K.,Pon, N.G.,Valkova-Valchanova, M.,Daldal, F.
X-Ray Structure of Rhodobacter Capsulatus Cytochrome bc (1): Comparison with its Mitochondrial and Chloroplast Counterparts.
Photosynth.Res., 81:251-275, 2004

PubMed Abstract: Ubihydroquinone: cytochrome (cyt)c oxidoreductase, or cyt bc (1), is a widespread, membrane integral enzyme that plays a crucial role during photosynthesis and respiration. It is one of the major contributors of the electrochemical proton gradient, which is subsequently used for ATP synthesis. The simplest form of the cyt bc (1) is found in bacteria, and it contains only the three ubiquitously conserved catalytic subunits: the Fe-S protein, cyt b and cyt c (1). Here we present a preliminary X-ray structure of Rhodobacter capsulatus cyt bc (1) at 3.8 A and compare it to the available structures of its homologues from mitochondria and chloroplast. Using the bacterial enzyme structure, we highlight the structural similarities and differences that are found among the three catalytic subunits between the members of this family of enzymes. In addition, we discuss the locations of currently known critical mutations, and their implications in terms of the cyt bc (1) catalysis.

PubMed: 16034531
DOI: 10.1023/B:PRES.0000036888.18223.0e

Experimental method

X-RAY DIFFRACTION (3.51 Å)