3PPU

Crystal structure of the glutathione-S-transferase Xi from Phanerochaete chrysosporium

Summary for 3PPU

• Entry DOI: 10.2210/pdb3ppu/pdb
• Descriptor: Glutathione-S-transferase, GLUTATHIONE (3 entities in total)
• Functional Keywords: gst fold, transferase
• Biological source: Phanerochaete chrysosporium (White-rot fungus)
• Total number of polymer chains: 2
• Total formula weight: 81468.98

Authors

Didierjean, C.,Prosper, P.,Favier, F. (deposition date: 2010-11-25, release date: 2010-12-22, Last modification date: 2013-04-24)

Primary citation

Meux, E.,Prosper, P.,Ngadin, A.,Didierjean, C.,Morel, M.,Dumarcay, S.,Lamant, T.,Jacquot, J.P.,Favier, F.,Gelhaye, E.
Glutathione transferases of Phanerochaete chrysosporium: S-glutathionyl-p-hydroquinone reductase belongs to a new structural class.
J.Biol.Chem., 286:9162-9173, 2011

PubMed Abstract: The white rot fungus Phanerochaete chrysosporium, a saprophytic basidiomycete, possesses a large number of cytosolic glutathione transferases, eight of them showing similarity to the Omega class. PcGSTO1 (subclass I, the bacterial homologs of which were recently proposed, based on their enzymatic function, to constitute a new class of glutathione transferase named S-glutathionyl-(chloro)hydroquinone reductases) and PcGSTO3 (subclass II related to mammalian homologs) have been investigated in this study. Biochemical investigations demonstrate that both enzymes are able to catalyze deglutathionylation reactions thanks to the presence of a catalytic cysteinyl residue. This reaction leads to the formation of a disulfide bridge between the conserved cysteine and the removed glutathione from their substrate. The substrate specificity of each isoform differs. In particular PcGSTO1, in contrast to PcGSTO3, was found to catalyze deglutathionylation of S-glutathionyl-p-hydroquinone substrates. The three-dimensional structure of PcGSTO1 presented here confirms the hypothesis that it belongs not only to a new biological class but also to a new structural class that we propose to name GST xi. Indeed, it shows specific features, the most striking ones being a new dimerization mode and a catalytic site that is buried due to the presence of long loops and that contains the catalytic cysteine.

PubMed: 21177852
DOI: 10.1074/jbc.M110.194548

Experimental method

X-RAY DIFFRACTION (2.3 Å)