1fcd

THE STRUCTURE OF FLAVOCYTOCHROME C SULFIDE DEHYDROGENASE FROM A PURPLE PHOTOTROPHIC BACTERIUM CHROMATIUM VINOSUM AT 2.5 ANGSTROMS RESOLUTION

spinqualitylabelsall models 1fcd, resolution 2.53Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1fcd is a 4 chain structure with sequence from "bacillus_vinosus"_(ehrenberg_1838)_trevisan_1889 "bacillus vinosus" (ehrenberg 1838) trevisan 1889. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FAD, HEM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CYSD_ALLVD] Diheme cytochrome that function as the electron transport subunit of sulfide dehydrogenase. 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 The structure of the heterodimeric flavocytochrome c sulfide dehydrogenase from Chromatium vinosum was determined at a resolution of 2.53 angstroms. It contains a glutathione reductase-like flavin-binding subunit and a diheme cytochrome subunit. The diheme cytochrome folds as two domains, each resembling mitochondrial cytochrome c, and has an unusual interpropionic acid linkage joining the two heme groups in the interior of the subunit. The active site of the flavoprotein subunit contains a catalytically important disulfide bridge located above the pyrimidine portion of the flavin ring. A tryptophan, threonine, or tyrosine side chain may provide a partial conduit for electron transfer to one of the heme groups located 10 angstroms from the flavin. The structure of flavocytochrome c sulfide dehydrogenase from a purple phototrophic bacterium.,Chen ZW, Koh M, Van Driessche G, Van Beeumen JJ, Bartsch RG, Meyer TE, Cusanovich MA, Mathews FS Science. 1994 Oct 21;266(5184):430-2. PMID:7939681 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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