5ZF1
Molecular structure of a novel 5,10-methylenetetrahydrofolate dehydrogenase from the silkworm, Bombyx mori
5ZF1 の概要
| エントリーDOI | 10.2210/pdb5zf1/pdb |
| 分子名称 | 5,10-methylenetetrahydrofolate dehydrogenase, SULFATE ION, 1,2-ETHANEDIOL, ... (4 entities in total) |
| 機能のキーワード | lepidoptera, 5, 10-methylenetetrahydrofolate dehydrogenase, nadp+, serine, oxidoreductase |
| 由来する生物種 | Bombyx mori (Silk moth) |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 66094.11 |
| 構造登録者 | Haque, R.,Higashiura, A.,Nakagawa, A.,Yamamoto, K. (登録日: 2018-03-02, 公開日: 2019-01-23, 最終更新日: 2024-03-27) |
| 主引用文献 | Haque, M.R.,Higashiura, A.,Nakagawa, A.,Hirowatari, A.,Furuya, S.,Yamamoto, K. Molecular structure of a 5,10-methylenetetrahydrofolate dehydrogenase from the silkwormBombyx mori. FEBS Open Bio, 9:618-628, 2019 Cited by PubMed Abstract: The enzyme 5,10-methylenetetrahydrofolate dehydrogenase (MTHFD) is essential for the production of certain amino acids (glycine, serine, and methionine) and nucleic acids (thymidylate and purine). Here, we identified a cDNA encoding this enzyme from the silkworm . The recombinant MTHFD (bmMTHFD) expressed in recognized 5,10-methylenetetrahydrofolate and 5,10-methenyltetrahydrofolate as substrate in the presence of NADP as well as NAD . The bmMTHFD structure was determined at a resolution of 1.75 Å by X-ray crystallography. Site-directed mutagenesis indicated that the amino acid residue Tyr49 contributed to its catalytic activity. Our findings provide insight into the mechanism underlying the activity of MTHFD from and potentially other insects and may therefore facilitate the development of inhibitors specific to MTHFD as insecticides. PubMed: 30984537DOI: 10.1002/2211-5463.12595 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.75 Å) |
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