1GWC

The structure of a tau class glutathione S-transferase from wheat, active in herbicide detoxification

1GWC の概要

• エントリーDOI: 10.2210/pdb1gwc/pdb
• 分子名称: GLUTATHIONE S-TRANSFERASE TSI-1, S-HEXYLGLUTATHIONE, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: transferase, glutathione s-transferase, herbicide detoxification, plant, tau class
• 由来する生物種: AEGILOPS TAUSCHII (BREAD WHEAT)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 76044.86

構造登録者

Thom, R.,Cummins, I.,Dixon, D.P.,Edwards, R.,Cole, D.J.,Lapthorn, A.J. (登録日: 2002-03-14, 公開日: 2002-06-06, 最終更新日: 2023-12-13)

主引用文献

Thom, R.,Cummins, I.,Dixon, D.P.,Edwards, R.,Cole, D.J.,Lapthorn, A.J.
Structure of a Tau Class Glutathione S-Transferase from Wheat Active in Herbicide Detoxification
Biochemistry, 41:7008-, 2002

PubMed Abstract: Glutathione S-transferases (GSTs) from the phi (GSTF) and tau (GSTU) classes are unique to plants and play important roles in stress tolerance and secondary metabolism as well as catalyzing the detoxification of herbicides in crops and weeds. We have cloned and functionally characterized a group of GSTUs from wheat treated with fenchlorazole-ethyl, a herbicide safener. One of these enzymes, TaGSTU4-4, was highly active in conjugating the chemically distinct wheat herbicides fenoxaprop and dimethenamid. The structure of TaGSTU4-4 has been determined at 2.2 A resolution in complex with S-hexylglutathione. This enzyme is the first tau class GST structure to be determined and most closely resembles the omega class GSTs, but without the unique N-terminal extension or active site cysteine. The X-ray structure identifies key amino acid residues in the hydrophobic binding site and provides insights into the substrate specificity of these enzymes.

PubMed: 12033934
DOI: 10.1021/BI015964X

実験手法

X-RAY DIFFRACTION (2.25 Å)