4YH2

Glutathione Transferase E6 from Drosophila melanogaster

4YH2 の概要

• エントリーDOI: 10.2210/pdb4yh2/pdb
• 分子名称: Glutathione S transferase E6, GLUTATHIONE (3 entities in total)
• 機能のキーワード: transferase, drosophila
• 由来する生物種: Drosophila melanogaster (Fruit fly)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 101399.55

構造登録者

Wongsantichon, J.,Robinson, R.C.,Ketterman, A.J. (登録日: 2015-02-26, 公開日: 2016-02-10, 最終更新日: 2024-03-20)

主引用文献

Wongsantichon, J.,Robinson, R.C.,Ketterman, A.J.
Epsilon glutathione transferases possess a unique class-conserved subunit interface motif that directly interacts with glutathione in the active site
Biosci.Rep., 35:-, 2015

PubMed Abstract: Epsilon class glutathione transferases (GSTs) have been shown to contribute significantly to insecticide resistance. We report a new Epsilon class protein crystal structure from Drosophila melanogaster for the glutathione transferase DmGSTE6. The structure reveals a novel Epsilon clasp motif that is conserved across hundreds of millions of years of evolution of the insect Diptera order. This histidine-serine motif lies in the subunit interface and appears to contribute to quaternary stability as well as directly connecting the two glutathiones in the active sites of this dimeric enzyme.

PubMed: 26487708
DOI: 10.1042/BSR20150183

実験手法

X-RAY DIFFRACTION (1.72 Å)