4G10
LigG from Sphingobium sp. SYK-6 is related to the glutathione transferase omega class
4G10 の概要
エントリーDOI | 10.2210/pdb4g10/pdb |
分子名称 | Glutathione S-transferase homolog, GLUTATHIONE, ACETATE ION, ... (5 entities in total) |
機能のキーワード | thioredoxin fold, transferase |
由来する生物種 | Sphingomonas paucimobilis |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 31202.97 |
構造登録者 | Meux, E.,Prosper, P.,Masai, E.,Mulliert Carlin, G.,Dumarcay, S.,Morel, M.,Didierjean, C.,Gelhaye, E.,Favier, F. (登録日: 2012-07-10, 公開日: 2012-10-03, 最終更新日: 2017-11-15) |
主引用文献 | Meux, E.,Prosper, P.,Masai, E.,Mulliert, G.,Dumarcay, S.,Morel, M.,Didierjean, C.,Gelhaye, E.,Favier, F. Sphingobium sp. SYK-6 LigG involved in lignin degradation is structurally and biochemically related to the glutathione transferase omega class. Febs Lett., 586:3944-3950, 2012 Cited by PubMed Abstract: SpLigG is one of the three glutathione transferases (GSTs) involved in the process of lignin breakdown in the soil bacterium Sphingobium sp. SYK-6. Sequence comparisons showed that SpLigG and several proteobacteria homologues form an independent cluster within cysteine-containing GSTs. The relationship between SpLigG and other GSTs was investigated. The X-ray structure and biochemical properties of SpLigG indicate that this enzyme belongs to the omega class of glutathione transferases. However, the hydrophilic substrate binding site of SpLigG, together with its known ability to stereoselectively deglutathionylate the physiological substrate α-glutathionyl-β-hydroxypropiovanillone, argues for broadening the definition of the omega class. PubMed: 23058289DOI: 10.1016/j.febslet.2012.09.036 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.2 Å) |
構造検証レポート
検証レポート(詳細版)をダウンロード