2QJP

Crystal structure of wild type rhodobacter sphaeroides with stigmatellin and antimycin inhibited

Summary for 2QJP

• Entry DOI: 10.2210/pdb2qjp/pdb
• Related: 1KB9 1NTK 1ZRT 1l0n 1sqx 2QJK
• Descriptor: Cytochrome b, FE2/S2 (INORGANIC) CLUSTER, Cytochrome c1, ... (11 entities in total)
• Functional Keywords: cytochrome b with 8 tm helices, one c-term tm in cytochrome c1 and an n-term tm in the iron-sulfur-protein (rieske), electron transport, heme, membrane, metal-binding, respiratory chain, transmembrane, transport, 2fe-2s, inner membrane, oxidoreductase
• Biological source: Rhodobacter sphaeroides; More
• Total number of polymer chains: 12
• Total formula weight: 397597.70

Authors

Esser, L.,Xia, D. (deposition date: 2007-07-08, release date: 2007-12-25, Last modification date: 2024-10-30)

Primary citation

Esser, L.,Elberry, M.,Zhou, F.,Yu, C.A.,Yu, L.,Xia, D.
Inhibitor-complexed structures of the cytochrome bc1 from the photosynthetic bacterium Rhodobacter sphaeroides.
J.Biol.Chem., 283:2846-2857, 2008

PubMed Abstract: The cytochrome bc(1) complex (bc(1)) 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 bc(1) complexes from the photosynthetic purple bacterium Rhodobacter sphaeroides (Rsbc(1)), stabilized with the quinol oxidation (Q(P)) site inhibitor stigmatellin alone or in combination with the quinone reduction (Q(N)) site inhibitor antimycin, were determined. The high quality electron density permitted assignments of a new metal-binding site to the cytochrome c(1) subunit and a number of lipid and detergent molecules. Structural differences between Rsbc(1) 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 bc(1) complex are derived from analyses of 10 independent molecules in various crystal forms and from comparisons with mitochondrial complexes.

PubMed: 18039651
DOI: 10.1074/jbc.M708608200

Experimental method

X-RAY DIFFRACTION (2.6 Å)