title: 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.
authors.affiliation: Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, University of Tokyo, Bunkyo-ku, Tokyo, 113-8657, Japan.|Tokyo University of Marine Science and Technology, Minato-ku, Tokyo, 108-8477, Japan.
authors.forename: Masahiko
authors.initials: M
authors.lastname: Okai
authors.affiliation: Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, University of Tokyo, Bunkyo-ku, Tokyo, 113-8657, Japan.
authors.forename: Woo Cheol
authors.initials: WC
authors.lastname: Lee
authors.affiliation: Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, University of Tokyo, Bunkyo-ku, Tokyo, 113-8657, Japan.|Food Processing Institute, Heilongjiang Academy of Agricultural Sciences, Nangang District, Harbin, 150086, China.
authors.forename: Li-Jun
authors.initials: LJ
authors.lastname: Guan
authors.affiliation: Department of Biotechnology, Tottori University, Tottori, 680-8552, Japan.
authors.forename: Takashi
authors.initials: T
authors.lastname: Ohshiro
authors.affiliation: Department of Biotechnology, Tottori University, Tottori, 680-8552, Japan.
authors.forename: Yoshikazu
authors.initials: Y
authors.lastname: Izumi
authors.affiliation: Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, University of Tokyo, Bunkyo-ku, Tokyo, 113-8657, Japan.
authors.forename: Masaru
authors.identifier: 0000-0001-5072-2480
authors.initials: M
authors.lastname: Tanokura
mesh_terms: D000595:Amino Acid Sequence; D001120:Arginine / Q000737:chemistry / Q000378:metabolism; D001412:Bacillus subtilis / Q000737:chemistry* / Q000201:enzymology; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D001665:Binding Sites; D001713:Biphenyl Compounds / Q000737:chemistry* / Q000378:metabolism; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D015870:Gene Expression; D018698:Glutamic Acid / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D000587:Oxidoreductases Acting on CH-NH Group Donors / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D010105:Oxygenases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D011485:Protein Binding; D000072756:Protein Conformation, alpha-Helical; D000072757:Protein Conformation, beta-Strand; D054730:Protein Interaction Domains and Motifs; D055503:Protein Multimerization; D021122:Protein Subunits / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D016415:Sequence Alignment; D040681:Structural Homology, Protein; D013379:Substrate Specificity; D013876:Thiophenes / Q000737:chemistry* / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D001713:Biphenyl Compounds; D021122:Protein Subunits; D011994:Recombinant Proteins; D013876:Thiophenes; C058517:dibenzothiophene 5-oxide; D018698:Glutamic Acid; D001120:Arginine; C004369:2-phenylphenol; D010105:Oxygenases; C421210:dibenzothiophene sulfone monooxygenase; D000587:Oxidoreductases Acting on CH-NH Group Donors; C113720:EDTA monooxygenase
keywords: Bacillus subtilis; crystal structure; dibenzothiophene; monooxygenase; thermophilic bacteria