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6AK1

Crystal structure of DmoA from Hyphomicrobium sulfonivorans

6AK1 の概要
エントリーDOI10.2210/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
Cao, H.Y.,Wang, P.,Peng, M.,Li, C.Y. (登録日: 2018-08-28, 公開日: 2018-12-12, 最終更新日: 2023-11-22)
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: 30511672
DOI: 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)
構造検証レポート
Validation report summary of 6ak1
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-10-30に公開中

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