3WD6
Crystal structure of Bombyx mori omega-class glutathione transferase in complex with GSH
3WD6 の概要
| エントリーDOI | 10.2210/pdb3wd6/pdb |
| 分子名称 | Omega-class glutathione S-transferase, POTASSIUM ION, 1,2-ETHANEDIOL, ... (7 entities in total) |
| 機能のキーワード | electron sharing network, transferase, glutathione binding |
| 由来する生物種 | Bombyx mori (silk moth,silkworm) |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 121601.84 |
| 構造登録者 | Yamamoto, K.,Suzuki, M.,Higashiura, A.,Nakagawa, A. (登録日: 2013-06-07, 公開日: 2014-07-16, 最終更新日: 2024-03-20) |
| 主引用文献 | Yamamoto, K.,Suzuki, M.,Higashiura, A.,Nakagawa, A. Three-dimensional structure of a Bombyx mori Omega-class glutathione transferase. Biochem.Biophys.Res.Commun., 438:588-593, 2013 Cited by PubMed Abstract: Glutathione transferases (GSTs) are major phase II detoxification enzymes that play central roles in the defense against various environmental toxicants as well as oxidative stress. Here we report the crystal structure of an Omega-class glutathione transferase of Bombyx mori, bmGSTO, to gain insight into its catalytic mechanism. The structure of bmGSTO complexed with glutathione determined at a resolution of 2.5Å reveals that it exists as a dimer and is structurally similar to Omega-class GSTs with respect to its secondary and tertiary structures. Analysis of a complex between bmGSTO and glutathione showed that bound glutathione was localized to the glutathione-binding site (G-site). Site-directed mutagenesis of bmGSTO mutants indicated that amino acid residues Leu62, Lys65, Lys77, Val78, Glu91 and Ser92 in the G-site contribute to catalytic activity. PubMed: 23939046DOI: 10.1016/j.bbrc.2013.08.011 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.5 Å) |
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