Structural highlights
Publication Abstract from PubMed
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 A. 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 alpha9-alpha12 helices in BdsA are closer to those of the closed form than those of the open form in the EDTA monooxygenase EmoA. Proteins 2017. (c) 2017 Wiley Periodicals, Inc.
Crystal structure of dibenzothiophene sulfone monooxygenase BdsA from Bacillus subtilis WU-S2B.,Okai M, Lee WC, Guan LJ, Ohshiro T, Izumi Y, Tanokura M Proteins. 2017 Feb 16. doi: 10.1002/prot.25267. PMID:28205250[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Okai M, Lee WC, Guan LJ, Ohshiro T, Izumi Y, Tanokura M. Crystal structure of dibenzothiophene sulfone monooxygenase BdsA from Bacillus subtilis WU-S2B. Proteins. 2017 Feb 16. doi: 10.1002/prot.25267. PMID:28205250 doi:http://dx.doi.org/10.1002/prot.25267
