1zrt

Rhodobacter capsulatus cytochrome bc1 complex with stigmatellin boundRhodobacter capsulatus cytochrome bc1 complex with stigmatellin bound

Structural highlights 1zrt is a 6 chain structure with sequence from "rhodonostoc_capsulatum"_molisch_1907 "rhodonostoc capsulatum" molisch 1907. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: , , , , , Related: 6xi0, 1pp9, 1kb9, 2qjy, 2yiu Gene: petB, cytB, RCAP_rcc02769 ("Rhodonostoc capsulatum" Molisch 1907), petC, RCAP_rcc02770 ("Rhodonostoc capsulatum" Molisch 1907), petA, fbcF, RCAP_rcc02768 ("Rhodonostoc capsulatum" Molisch 1907) Activity: Quinol--cytochrome-c reductase, with EC number 7.1.1.8 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CYB_RHOCB] Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. [UCRI_RHOCB] Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. [CY1_RHOCB] Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. c1 functions as an electron donor to cytochrome c. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. X-Ray Structure of Rhodobacter Capsulatus Cytochrome bc (1): Comparison with its Mitochondrial and Chloroplast Counterparts.,Berry EA, Huang LS, Saechao LK, Pon NG, Valkova-Valchanova M, Daldal F Photosynth Res. 2004;81(3):251-75. PMID:16034531 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cytochrome C 3D structures Cytochrome bc1 complex

spinqualitylabelsall models 1zrt, resolution 3.51Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image