Premium
Structural insights into the stabilization of active, tetrameric DszC by its C‐terminus
Author(s) -
Zhang Liang,
Duan Xiaolu,
Zhou Daming,
Dong Zhe,
Ji Kaihua,
Meng Wuyi,
Li Guoqiang,
Li Xin,
Yang Haitao,
Ma Ting,
Rao Zihe
Publication year - 2014
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.24638
Subject(s) - dibenzothiophene , enzyme , chemistry , active site , substrate (aquarium) , stereochemistry , biochemistry , monooxygenase , catalysis , biology , cytochrome p450 , ecology
Dibenzothiophene (DBT) is a typical sulfur‐containing compound found in fossil fuels. This compound and its derivatives are resistant to the hydrodesulfurization method often used in industry, but they are susceptible to enzymatic desulfurization via the 4S pathway, which is a well‐studied biochemical pathway consisting of four enzymes. DBT monooxygenase (DszC) from Rhodococcus erythropolis is involved in the first step of the 4S pathway. We determined the crystal structure of DszC, which reveals that, in contrast to several homologous proteins, the C‐terminus (410–417) of DszC participates in the stabilization of the substrate‐binding pocket. Analytical ultracentrifugation analysis and enzymatic assays confirmed that the C‐terminus is important for the stabilization of the active conformation of the substrate‐binding pocket and the tetrameric state. Therefore, the C‐terminus of DszC plays a significant role in the catalytic activity of this enzyme. Proteins 2014; 82:2733–2743. © 2014 Wiley Periodicals, Inc.