Crystal structure of dibenzothiophene sulfone monooxygenase BdsA from Bacillus subtilis WU-S2B.
Proteins
; 85(6): 1171-1177, 2017 06.
Article
em En
| MEDLINE
| ID: mdl-28205250
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; 851171-1177. © 2017 Wiley Periodicals, Inc.
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MEDLINE
Assunto principal:
Oxigenases
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Tiofenos
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Bacillus subtilis
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Proteínas de Bactérias
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Compostos de Bifenilo
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Subunidades Proteicas
Idioma:
En
Ano de publicação:
2017
Tipo de documento:
Article