6AK1
Crystal structure of DmoA from Hyphomicrobium sulfonivorans
6AK1 の概要
エントリーDOI | 10.2210/pdb6ak1/pdb |
分子名称 | Dimethyl-sulfide monooxygenase (2 entities in total) |
機能のキーワード | dimethylsulfide monooxygenase, tim barrel, oxidoreductase |
由来する生物種 | Hyphomicrobium sulfonivorans |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 108497.33 |
構造登録者 | |
主引用文献 | Cao, H.Y.,Wang, P.,Peng, M.,Shao, X.,Chen, X.L.,Li, C.Y. Crystal structure of the dimethylsulfide monooxygenase DmoA from Hyphomicrobium sulfonivorans. Acta Crystallogr.,Sect.F, 74:781-786, 2018 Cited by PubMed Abstract: DmoA is a monooxygenase which uses dioxygen (O) and reduced flavin mononucleotide (FMNH) 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. PubMed: 30511672DOI: 10.1107/S2053230X18015844 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.284 Å) |
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