6GCB

Crystal structure of glutathione transferase Xi 3 from Trametes versicolor in complex with glutathione

Summary for 6GCB

• Entry DOI: 10.2210/pdb6gcb/pdb
• Descriptor: Glutathione transferase Xi 3 from Trametes versicolor, GLUTATHIONE (3 entities in total)
• Functional Keywords: glutathione transferase, transferase
• Biological source: Trametes versicolor
• Total number of polymer chains: 2
• Total formula weight: 74940.94

Authors

Schwartz, M.,Favier, F.,Didierjean, C. (deposition date: 2018-04-17, release date: 2018-08-29, Last modification date: 2024-01-17)

Primary citation

Schwartz, M.,Perrot, T.,Deroy, A.,Roret, T.,Morel-Rouhier, M.,Mulliert, G.,Gelhaye, E.,Favier, F.,Didierjean, C.
Trametes versicolor glutathione transferase Xi 3, a dual Cys-GST with catalytic specificities of both Xi and Omega classes.
FEBS Lett., 592:3163-3172, 2018

PubMed Abstract: 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 biochemical and structural analysis 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. An in-depth 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 saprophytic fungi and ascomycetes.

PubMed: 30112765
DOI: 10.1002/1873-3468.13224

Experimental method

X-RAY DIFFRACTION (1.795 Å)