5XKC

Crystal structure of dibenzothiophene sulfone monooxygenase BdsA at 2.2 angstrome

5XKC の概要

• エントリーDOI: 10.2210/pdb5xkc/pdb
• 関連するPDBエントリー: 5XKD
• 分子名称: Dibenzothiophene desulfurization enzyme A (2 entities in total)
• 機能のキーワード: dibenzothiophene desulfurization enzyme, monooxygenase, oxidoreductase
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 198838.92

構造登録者

Gu, L.,Su, T.,Liu, S.,Su, J. (登録日: 2017-05-07, 公開日: 2018-05-09, 最終更新日: 2023-11-22)

主引用文献

Su, T.,Su, J.,Liu, S.,Zhang, C.,He, J.,Huang, Y.,Xu, S.,Gu, L.
Structural and Biochemical Characterization of BdsA fromBacillus subtilisWU-S2B, a Key Enzyme in the "4S" Desulfurization Pathway.
Front Microbiol, 9:231-231, 2018

PubMed Abstract: Dibenzothiophene (DBT) and their derivatives, accounting for the major part of the sulfur components in crude oil, make one of the most significant pollution sources. The DBT sulfone monooxygenase BdsA, one of the key enzymes in the "4S" desulfurization pathway, catalyzes the oxidation of DBT sulfone to 2'-hydroxybiphenyl 2-sulfonic acid (HBPSi). Here, we determined the crystal structure of BdsA from WU-S2B, at the resolution of 2.2 Å, and the structure of the BdsA-FMN complex at 2.4 Å. BdsA and the BdsA-FMN complex exist as tetramers. DBT sulfone was placed into the active site by molecular docking. Seven residues (Phe12, His20, Phe56, Phe246, Val248, His316, and Val372) are found to be involved in the binding of DBT sulfone. The importance of these residues is supported by the study of the catalytic activity of the active site variants. Structural analysis and enzyme activity assay confirmed the importance of the right position and orientation of FMN and DBT sulfone, as well as the involvement of Ser139 as a nucleophile in catalysis. This work combined with our previous structure of DszC provides a systematic structural basis for the development of engineered desulfurization enzymes with higher efficiency and stability.

PubMed: 29497411
DOI: 10.3389/fmicb.2018.00231

実験手法

X-RAY DIFFRACTION (2.209 Å)