%0 Generic %A Schwartz, Mathieu %A Perrot, Thomas %A Deroy, Aurélie %A Roret, Thomas %A Morel-Rouhier, Melanie %A Mulliert, Guillermo %A Gelhaye, Eric %A Favier, Frédérique %A Didierjean, Claude %D 2018 %T Dataset for: Trametes versicolor Glutathione Transferase Xi 3, a dual Cys-GST with catalytic specificities of both Xi and Omega classes %U https://wiley.figshare.com/articles/dataset/Dataset_for_Trametes_versicolor_Glutathione_Transferase_Xi_3_a_dual_Cys-GST_with_catalytic_specificities_of_both_Xi_and_Omega_classes/6960452 %R 10.6084/m9.figshare.6960452.v1 %2 https://wiley.figshare.com/ndownloader/files/12767468 %K Glutathione transferase %K Dual Activity %K Crystallography %K Biophysics %K Synthetic Biology %K Biochemistry %K Plant Biology %K Virology %K Receptors and Membrane Biology %K Computational Biology %K Immunology %K Neuroscience %K Cell Development, Proliferation and Death %K Molecular Biology %K Evolutionary Biology %K Signal Transduction %K Cancer Cell Biology %K Systems Biology %K Structural Biology %X Glutathione transferases (GSTs) from the Xi and Omega classes have a catalytic cysteine residue which gives them reductase activities. Until now, they have been assigned distinct substrates. While Xi GSTs specifically reduce glutathionyl-(hydro)quinones, Omega GSTs are specialized in the reduction of glutathionyl-acetophenones. Here we present the study of TvGSTX1 and TvGSTX3 isoforms from the wood-degrading fungus Trametes versicolor. TvGSTX1 reduces GS-menadione as expected while TvGSTX3 reduces both Xi and Omega substrates. A structural analysis indicates a broader active site for TvGSTX3 due to specific differences in the nature of the residues situated in the C-terminal helix α9. This feature could explain the catalytic duality of TvGSTX3. Based on phylogenetic analysis we propose that this duality might exist in other fungi. %I Wiley