4F03

Crystal structure of the glutathione transferase GTE1 from Phanerochaete chrysosporium

4F03 の概要

• エントリーDOI: 10.2210/pdb4f03/pdb
• 関連するPDBエントリー: 4G19
• 分子名称: Glutathione transferase, SULFATE ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: gst fold, glutathione, transferase
• 由来する生物種: Phanerochaete chrysosporium
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 116738.68

構造登録者

Didierjean, C.,Favier, F.,Prosper, P. (登録日: 2012-05-03, 公開日: 2012-09-26, 最終更新日: 2024-11-20)

主引用文献

Mathieu, Y.,Prosper, P.,Buee, M.,Dumarcay, S.,Favier, F.,Gelhaye, E.,Gerardin, P.,Harvengt, L.,Jacquot, J.P.,Lamant, T.,Meux, E.,Mathiot, S.,Didierjean, C.,Morel, M.
Characterization of a Phanerochaete chrysosporium Glutathione Transferase Reveals a Novel Structural and Functional Class with Ligandin Properties.
J.Biol.Chem., 287:39001-39011, 2012

PubMed Abstract: Glutathione S-transferases (GSTs) form a superfamily of multifunctional proteins with essential roles in cellular detoxification processes. A new fungal specific class of GST has been highlighted by genomic approaches. The biochemical and structural characterization of one isoform of this class in Phanerochaete chrysosporium revealed original properties. The three-dimensional structure showed a new dimerization mode and specific features by comparison with the canonical GST structure. An additional β-hairpin motif in the N-terminal domain prevents the formation of the regular GST dimer and acts as a lid, which closes upon glutathione binding. Moreover, this isoform is the first described GST that contains all secondary structural elements, including helix α4' in the C-terminal domain, of the presumed common ancestor of cytosolic GSTs (i.e. glutaredoxin 2). A sulfate binding site has been identified close to the glutathione binding site and allows the binding of 8-anilino-1-naphtalene sulfonic acid. Competition experiments between 8-anilino-1-naphtalene sulfonic acid, which has fluorescent properties, and various molecules showed that this GST binds glutathionylated and sulfated compounds but also wood extractive molecules, such as vanillin, chloronitrobenzoic acid, hydroxyacetophenone, catechins, and aldehydes, in the glutathione pocket. This enzyme could thus function as a classical GST through the addition of glutathione mainly to phenethyl isothiocyanate, but alternatively and in a competitive way, it could also act as a ligandin of wood extractive compounds. These new structural and functional properties lead us to propose that this GST belongs to a new class that we name GSTFuA, for fungal specific GST class A.

PubMed: 23007392
DOI: 10.1074/jbc.M112.402776

実験手法

X-RAY DIFFRACTION (1.8 Å)