5TLC

Crystal structure of BdsA from Bacillus subtilis WU-S2B

Summary for 5TLC

• Entry DOI: 10.2210/pdb5tlc/pdb
• Descriptor: Dibenzothiophene desulfurization enzyme A (2 entities in total)
• Functional Keywords: monooxygenase, oxidoreductase
• Biological source: Bacillus subtilis
• Total number of polymer chains: 4
• Total formula weight: 198838.92

Authors

Okai, M.,Lee, W.C.,Tanokura, M. (deposition date: 2016-10-11, release date: 2017-05-03, Last modification date: 2024-03-20)

Primary citation

Okai, M.,Lee, W.C.,Guan, L.J.,Ohshiro, T.,Izumi, Y.,Tanokura, M.
Crystal structure of dibenzothiophene sulfone monooxygenase BdsA from Bacillus subtilis WU-S2B
Proteins, 85:1171-1177, 2017

PubMed 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.

PubMed: 28205250
DOI: 10.1002/prot.25267

Experimental method

X-RAY DIFFRACTION (2.8 Å)