Crystal structure of dibenzothiophene sulfone monooxygenase BdsA from Bacillus subtilis WU‐S2B

Abstract

The dibenzothiophene (DBT) sulfone monooxygenase BdsA from Bacillus subtilis WU-S2B catalyzes the conversion of DBT sulfone to 2'-hydroxybiphenyl 2-sulfinate. We report the crystal structures of BdsA at a resolution of 2.80 Å. BdsA exists as a homotetramer with a dimer-of-dimers configuration in the crystal, and the interaction between E288 and R296 in BdsA is important for tetramer formation. A structural comparison with homologous proteins shows that the orientation and location of the α9-α12 helices in BdsA are closer to those of the closed form than those of the open form in the EDTA monooxygenase EmoA. Proteins 2017; 85:1171-1177. © 2017 Wiley Periodicals, Inc.

Crystal structure of the dimethylsulfide monooxygenase DmoA from Hyphomicrobium sulfonivorans

“…1c), which are all located between the inside -strands and the outside -helices. These additional insertions are also observed in the long-chain alkane monooxygenase LadA (Li et al, 2008) and the dibenzothiophene sulfone monooxygenase BdsA (Okai et al, 2017; PDB entry 5tlc). The five additional insertions in DmoA are named AI1 to AI5.…”

Structural and Biochemical Characterization of BdsA from Bacillus subtilis WU-S2B, a Key Enzyme in the “4S” Desulfurization Pathway

“…The three-dimensional structure of BdsA is essential for elucidating the catalytic mechanism of the DBT sulfone monooxygenation. Recently, the crystal structure of BdsA was reported by Masahiko at a resolution of 2.8 Å ( Okai et al, 2017 ), which provides architectural information and comparison with the homologous proteins of BdsA. However, the study by Masahiko did not give the structure of the complex with FMN or the substrate.…”

Formicamycin biosynthesis involves a unique reductive ring contraction

“…Structural homology searches predicted ForY to be a TIM beta/alpha barrel oxidoreductase (Table 1), homologues of which typically utilize avin cofactors to perform redox chemistry. [13][14][15][16][17] The genes forZ and forAA encode a MarR family transcriptional regulator and an MFS family transporter respectively.…”

“…Chemical skeletons of fasamycins(1)(2)(3) and formicamycins (4-16) isolated from S. formicae KY5, and Baeyer-Villiger lactone intermediates(17)(18)(19)(20)(21) isolated from the S. formicae DforY mutant in this study (for detailed substituent variations including halogenation or Omethylation, seeFig. S1 †).…”