6UUG

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

Summary for 6UUG

• Entry DOI: 10.2210/pdb6uug/pdb
• Related: 6U76
• Descriptor: Putative dehydrogenase (2 entities in total)
• Functional Keywords: two-component flavin-dependent monooxygenase, methyl sulfur assimilation, dimethylsulfide, global sulfur cycle, flavoprotein
• Biological source: Pseudomonas fluorescens (strain Pf0-1)
• Total number of polymer chains: 2
• Total formula weight: 92516.02

Authors

Soule, J.,Gnann, A.D.,Gonzalez, R.,Parker, M.J.,McKenna, K.C.,Nguyen, S.V.,Phan, N.T.,Wicht, D.K.,Dowling, D.P. (deposition date: 2019-10-30, release date: 2019-12-04, Last modification date: 2023-10-11)

Primary citation

Soule, J.,Gnann, A.D.,Gonzalez, R.,Parker, M.J.,McKenna, K.C.,Nguyen, S.V.,Phan, N.T.,Wicht, D.K.,Dowling, D.P.
Structure and function of the two-component flavin-dependent methanesulfinate monooxygenase within bacterial sulfur assimilation.
Biochem.Biophys.Res.Commun., 522:107-112, 2020

PubMed Abstract: 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 (DMSO) assimilation: SfnG converts DMSO 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 DMSO.

PubMed: 31753487
DOI: 10.1016/j.bbrc.2019.11.008

Experimental method

X-RAY DIFFRACTION (1.685 Å)