6hpe

Crystal structure of glutathione transferase Omega 3S from Trametes versicolor in complex with the glutathione adduct of phenethyl-isothiocyanate

spinqualitylabelsall models 6hpe, resolution 1.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6hpe is a 2 chain structure with sequence from Trametes versicolor. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.45Å Ligands: CA, GOL, GVX, PEG, PG4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A384E145_TRAVE Publication Abstract from PubMed Trametes versicolor glutathione transferase Omega 3S (TvGSTO3S) catalyzes the conjugation of isothiocyanates (ITC) with glutathione (GSH). Previously, this isoform was investigated in depth both biochemically and structurally. Structural analysis of complexes revealed the presence of a glutathione binding site (G site) and a deep hydrophobic binding site (H site) able to bind plant polyphenols. In the present study, crystals of apo TvGSTO3S were soaked with GS-PEITC, the product of the reaction between glutathione (GSH) and phenethyl-isothiocyanate (PEITC). On the basis of this crystal structure, we show that the phenethyl moiety binds in a new site at loop beta2 -alpha2 while the glutathionyl part exhibits a particular conformation that occupies both the G site and the entrance to the H site. This binding mode is allowed by a conformational change of the loop beta2 -alpha2 at the enzyme active site. It forms a hydrophobic slit that stabilizes the phenethyl group at a distinct site from the previously described H site. Structural comparison of TvGSTO3S with drosophila DmGSTD2 suggests that this flexible loop could be the region that binds PEITC for both isoforms. These structural features are discussed in a catalytic context. The structure of Trametes versicolor Glutathione Transferase Omega 3S bound to its conjugation product GS-PEITC reveals plasticity of its active site.,Schwartz M, Perrot T, Morel-Rouhier M, Mulliert G, Gelhaye E, Didierjean C, Favier F Protein Sci. 2019 Apr 10. doi: 10.1002/pro.3620. PMID:30972861 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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