3w79 | pdb_00003w79

Crystal Structure of azoreductase AzrC in complex with sulfone-modified azo dye Orange I

spinqualitylabelsall models 3w79, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3w79 is a 4 chain structure with sequence from Bacillus sp. B29. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.4Å Ligands: FMN, ORI Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function C0STY1_9BACI Catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. Requires NADH, but not NADPH, as an electron donor for its activity (By similarity).[HAMAP-Rule:MF_01216][SAAS:SAAS003680_004_018232] Publication Abstract from PubMed Azo dyes are major synthetic dyestuffs with one or more azo bonds and are widely used for various industrial purposes. The biodegradation of residual azo dyes via azoreductase-catalyzed cleavage is very efficient as the initial step of wastewater treatment. The structures of the complexes of azoreductases with various substrates are therefore indispensable to understand their substrate specificity and catalytic mechanism. In this study, the crystal structures of AzrA and of AzrC complexed with Cibacron Blue (CB) and the azo dyes Acid Red 88 (AR88) and Orange I (OI) were determined. As an inhibitor/analogue of NAD(P)H, CB was located on top of flavin mononucleotide (FMN), suggesting a similar binding manner as NAD(P)H for direct hydride transfer to FMN. The structures of the AzrC-AR88 and AzrC-OI complexes showed two manners of binding for substrates possessing a hydroxy group at the ortho or the para position of the azo bond, respectively, while AR88 and OI were estimated to have a similar binding affinity to AzrC from ITC experiments. Although the two substrates were bound in different orientations, the hydroxy groups were located in similar positions, resulting in an arrangement of electrophilic C atoms binding with a proton/electron-donor distance of approximately 3.5 A to N5 of FMN. Catalytic mechanisms for different substrates are proposed based on the crystal structures and on site-directed mutagenesis analysis. Structures of AzrA and of AzrC complexed with substrate or inhibitor: insight into substrate specificity and catalytic mechanism.,Yu J, Ogata D, Gai Z, Taguchi S, Tanaka I, Ooi T, Yao M Acta Crystallogr D Biol Crystallogr. 2014 Feb;70(Pt 2):553-64. doi:, 10.1107/S1399004713030988. Epub 2014 Jan 31. PMID:24531489 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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