Author:
Cao Hai-Yan,Wang Peng,Peng Ming,Shao Xuan,Chen Xiu-Lan,Li Chun-Yang
Abstract
DmoA is a monooxygenase which uses dioxygen (O2) and reduced flavin mononucleotide (FMNH2) to catalyze the oxidation of dimethylsulfide (DMS). Although it has been characterized, the structure of DmoA remains unknown. Here, the crystal structure of DmoA was determined to a resolution of 2.28 Å and was compared with those of its homologues LadA and BdsA. The results showed that their overall structures are similar: they all share a conserved TIM-barrel fold which is composed of eight α-helices and eight β-strands. In addition, they all have five additional insertions. Detailed comparison showed that the structures have notable differences despite their high sequence similarity. The substrate-binding pocket of DmoA is smaller compared with those of LadA and BdsA.
Funder
National Key Research and Development Program of China
National Natural Science Foundation of China
Taishan Scholar Foundation of Shandong Province
Qingdao National Laboratory for Marine Science and Technology
National Postdoctoral Program for Innovative Talents
Natural Science Foundation of Jiangsu Province
Natural Science Foundation of Shandong Province
Shandong Province Postdoctoral Innovation Projects
Publisher
International Union of Crystallography (IUCr)
Subject
Condensed Matter Physics,Genetics,Biochemistry,Structural Biology,Biophysics
Cited by
8 articles.
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