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Crystal structures of apo‐DszC and FMN‐bound DszC from Rhodococcus erythropolis D‐1
Author(s) -
Guan LiJun,
Lee Woo Cheol,
Wang Shipeng,
Ohshiro Takashi,
Izumi Yoshikazu,
Ohtsuka Jun,
Tanokura Masaru
Publication year - 2015
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.13216
Subject(s) - protein data bank (rcsb pdb) , chemistry , active site , dibenzothiophene , stereochemistry , protein data bank , crystal structure , rhodococcus , cofactor , sulfur , enzyme , crystallography , protein structure , biochemistry , organic chemistry
The release of SO2 from petroleum products derived from crude oil, which contains sulfur compounds such as dibenzothiophene (DBT), leads to air pollution. The '4S' metabolic pathway catalyzes the sequential conversion of DBT to 2-hydroxybiphenyl via three enzymes encoded by the dsz operon in several bacterial species. DszC (DBT monooxygenase), from Rhodococcus erythropolis D-1 is involved in the first two steps of the '4S' pathway. Here, we determined the first crystal structure of FMN-bound DszC, and found that two distinct conformations occur in the loop region (residues 131-142) adjacent to the active site. On the basis of the DszC-FMN structure and the previously reported apo structures of DszC homologs, the binding site for DBT and DBT sulfoxide is proposed.