7vqk

Catalytic manifolds of a FMN-dependent oxidoreductase RubE7, expanding the functional diversity of the flavoenzyme superfamily

spinqualitylabelsall models 7vqk, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7vqk is a 2 chain structure with sequence from Streptomyces sp. KIB-H033. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: FMN, MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A3N6GWZ7_9ACTN Publication Abstract from PubMed Flavin-dependent enzymes enable a broad range of redox transformations and generally act as monofunctional and stereoselective catalysts. Herein, we report the investigation of a multifunctional and non-stereoselective FMN-dependent oxidoreductase RubE7 from the rubrolone biosynthetic pathway. Our study outlines a single RubE7-catalysed sequential reduction of three spatially distinct bonds in a tropolone ring and a reversible double-bond reduction and dehydrogenation. The crystal structure of IstO (a RubE7 homologue) with 2.0 A resolution reveals the location of the active site at the interface of two monomers, and the size of active site is large enough to permit both flipping and free rotation of the substrate, resulting in multiple nonselective reduction reactions. Molecular docking and site mutation studies demonstrate that His106 is oriented towards the substrate and is important for the reverse dehydrogenation reaction. Characterization of Multifunctional and Non-stereoselective Oxidoreductase RubE7/IstO, Expanding the Functional Diversity of the Flavoenzyme Superfamily.,Yan Y, Yu Z, Zhong W, Hou X, Tao Q, Cao M, Wang L, Cai X, Rao Y, Huang SX Angew Chem Int Ed Engl. 2022 May 2;61(19):e202200189. doi: , 10.1002/anie.202200189. Epub 2022 Feb 28. PMID:35191152 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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