4LMW

Crystal structure of glutathione transferase GSTFuA3 from Phanerochaete chrysosporium

4LMW の概要

• エントリーDOI: 10.2210/pdb4lmw/pdb
• 関連するPDBエントリー: 4F03 4G19 4LMV
• 分子名称: Glutathione transferase, FORMIC ACID (3 entities in total)
• 機能のキーワード: gst fold, glutathione transferase, transferase
• 由来する生物種: Phanerochaete chrysosporium
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29582.34

構造登録者

Didierjean, C.,Favier, F.,Prosper, P. (登録日: 2013-07-11, 公開日: 2014-05-28, 最終更新日: 2023-11-08)

主引用文献

Mathieu, Y.,Prosper, P.,Favier, F.,Harvengt, L.,Didierjean, C.,Jacquot, J.P.,Morel-Rouhier, M.,Gelhaye, E.
Diversification of fungal specific class a glutathione transferases in saprotrophic fungi.
Plos One, 8:e80298-e80298, 2013

PubMed Abstract: Glutathione transferases (GSTs) form a superfamily of multifunctional proteins with essential roles in cellular detoxification processes and endogenous metabolism. The distribution of fungal-specific class A GSTs was investigated in saprotrophic fungi revealing a recent diversification within this class. Biochemical characterization of eight GSTFuA isoforms from Phanerochaete chrysosporium and Coprinus cinereus demonstrated functional diversity in saprotrophic fungi. The three-dimensional structures of three P. chrysosporium isoforms feature structural differences explaining the functional diversity of these enzymes. Competition experiments between fluorescent probes, and various molecules, showed that these GSTs function as ligandins with various small aromatic compounds, derived from lignin degradation or not, at a L-site overlapping the glutathione binding pocket. By combining genomic data with structural and biochemical determinations, we propose that this class of GST has evolved in response to environmental constraints induced by wood chemistry.

PubMed: 24278272
DOI: 10.1371/journal.pone.0080298

実験手法

X-RAY DIFFRACTION (2.099 Å)