4F0B

Crystal structure of the glutathione transferase URE2P1 from Phanerochaete chrysosporium.

4F0B の概要

• エントリーDOI: 10.2210/pdb4f0b/pdb
• 関連するPDBエントリー: 4F0C
• 分子名称: THIOL TRANSFERASE, OXIDIZED GLUTATHIONE DISULFIDE, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: thiol transferase, gst fold, oxydized glutathione, transferase
• 由来する生物種: Phanerochaete chrysosporium
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 52289.45

構造登録者

Didierjean, C.,Favier, F.,Roret, T. (登録日: 2012-05-04, 公開日: 2013-06-12, 最終更新日: 2023-09-13)

主引用文献

Thuillier, A.,Roret, T.,Favier, F.,Gelhaye, E.,Jacquot, J.P.,Didierjean, C.,Morel-Rouhier, M.
Atypical features of a Ure2p glutathione transferase from Phanerochaete chrysosporium.
Febs Lett., 587:2125-2130, 2013

PubMed Abstract: Glutathione transferases (GSTs) are known to transfer glutathione onto small hydrophobic molecules in detoxification reactions. The GST Ure2pB1 from Phanerochaete chrysosporium exhibits atypical features, i.e. the presence of two glutathione binding sites and a high affinity towards oxidized glutathione. Moreover, PcUre2pB1 is able to efficiently deglutathionylate GS-phenacylacetophenone. Catalysis is not mediated by the cysteines of the protein but rather by the one of glutathione and an asparagine residue plays a key role in glutathione stabilization. Interestingly PcUre2pB1 interacts in vitro with a GST of the omega class. These properties are discussed in the physiological context of wood degrading fungi.

PubMed: 23711374
DOI: 10.1016/j.febslet.2013.05.031

実験手法

X-RAY DIFFRACTION (1.45 Å)