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2QJY

Crystal structure of rhodobacter sphaeroides double mutant with stigmatellin and UQ2

Summary for 2QJY
Entry DOI10.2210/pdb2qjy/pdb
DescriptorCytochrome b, FE2/S2 (INORGANIC) CLUSTER, CHLORIDE ION, ... (13 entities in total)
Functional Keywordscytochrome b, 8 tm helixces cytochrome c1, 1 c-term tm helix rieske, 1 n-term tm helix, oxidoreductase
Biological sourceRhodobacter sphaeroides
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Total number of polymer chains18
Total formula weight620444.94
Authors
Esser, L.,Xia, D. (deposition date: 2007-07-09, release date: 2007-12-25, Last modification date: 2023-08-30)
Primary citationEsser, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.4 Å)
Structure validation

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