Journal
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
Volume 85, Issue 6, Pages 1171-1177Publisher
WILEY
DOI: 10.1002/prot.25267
Keywords
dibenzothiophene; crystal structure; Bacillus subtilis; monooxygenase; thermophilic bacteria
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Funding
- Program to Disseminate the Tenure Tracking System
- National Project on Protein Structural and Functional Analyses
- Ministry of Education, Culture, Sports, Science and Technology of Japan
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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.
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