6uug

Structure of methanesulfinate monooxygenase MsuC from Pseudomonas fluorescens at 1.69 angstrom resolution

spinqualitylabelsall models 6uug, resolution 1.69Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6uug is a 2 chain structure with sequence from Pseudomonas fluorescens Pf0-1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.685Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q3K9A0_PSEPF Publication Abstract from PubMed Methyl sulfur compounds are a rich source of environmental sulfur for microorganisms, but their use requires redox systems. The bacterial sfn and msu operons contain two-component flavin-dependent monooxygenases for dimethylsulfone (DMSO2) assimilation: SfnG converts DMSO2 to methanesulfinate (MSI(-)), and MsuD converts methanesulfonate (MS(-)) to sulfite. However, the enzymatic oxidation of MSI(-) to MS(-) has not been demonstrated, and the function of the last enzyme of the msu operon (MsuC) is unresolved. We employed crystallographic and biochemical studies to identify the function of MsuC from Pseudomonas fluorescens. The crystal structure of MsuC adopts the acyl-CoA dehydrogenase fold with putative binding sites for flavin and MSI(-), and functional assays of MsuC in the presence of its oxidoreductase MsuE, FMN, and NADH confirm the enzymatic generation of MS(-). These studies reveal that MsuC converts MSI(-) to MS(-) in sulfite biosynthesis from DMSO2. Structure and function of the two-component flavin-dependent methanesulfinate monooxygenase within bacterial sulfur assimilation.,Soule J, Gnann AD, Gonzalez R, Parker MJ, McKenna KC, Nguyen SV, Phan NT, Wicht DK, Dowling DP Biochem Biophys Res Commun. 2019 Nov 18. pii: S0006-291X(19)32128-X. doi:, 10.1016/j.bbrc.2019.11.008. PMID:31753487 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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