文献类型： 外文期刊

作者： Okai, Masahiko ¹ ; Lee, Woo Cheol ¹ ; Guan, Li-Jun ¹ ; Ohshiro, Takashi ⁴ ; Izumi, Yoshikazu ⁴ ; Tanokura, Masaru ¹ ;

作者机构： 1.Univ Tokyo, Grad Sch Agr & Life Sci, Dept Appl Biol Chem, Bunkyo Ku, 1-1-1 Yayoi, Tokyo 1138657, Japan

2.Tokyo Univ Marine Sci & Technol, Minato Ku, Tokyo 1088477, Japan

3.Heilongjiang Acad Agr Sci, Food Proc Inst, Harbin 150086, Peoples R China

4.Tottori Univ, Dept Biotechnol, Tottori 6808552, Japan

关键词： dibenzothiophene;crystal structure;Bacillus subtilis;monooxygenase;thermophilic bacteria

期刊名称：PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS （ 影响因子：3.756； 五年影响因子：2.752 ）

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收录情况： SCI

摘要： 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 angstrom. 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 alpha 9-alpha 12 helices in BdsA are closer to those of the closed form than those of the open form in the EDTA monooxygenase EmoA. (C) 2017 Wiley Periodicals, Inc.