@text
      Glutathione S-transferases (GSTs) conjugate cytotoxic proteins to glutathione (GSH), thereby inhibiting the cytotoxins activity.  There are four known classes of GSTs in  plants: theta, zeta, tau and phi.  The GSTs are classified according to their amino acid sequence.  The phi and tau classes are unique to plants, but homologs of the GSTs in  zeta and theta classes exist in other organisms.
     Ascribed roles of GSTs classified in either phi or tau groups include oxidative stress tolerance, cell signaling, transport of toxic secondary products and herbicide detoxification.  Herbicide detoxification occurs by conjugation of the herbicide to GSH by the GST; GSTs in phi and tau classes are responsible for the detoxification of different herbicides.  In contrast to phi class GSTs, tau class GSTs share only 25% homology with other GSTs and have not been crystallized.  Information obtained by studying the structure of tau class and other GSTs can be utilized to determine specificity of the proteins for substrates.  Additionally, transgenic plants could be created that express the GSTs and provide a benefit to the agricultural community. 
     Presented in this kinemage is the structure of a tau class GST isolated from Triticum aestivum (wheat) (Thom et al., 2002).  The structure was determined by x-ray crystallography after incubation of the GST with an herbicide, separation by various chromatography techniques and crystallization in the presence of the inhibitor S-hexylglutathione.  

Thom R, Cummins I, Dixon DP, Edwards R, Cole DJ, Lapthorn AJ. 2002. Structure of a Tau Class Glutathione S-Transferase from Wheat Active in Herbicide Detoxification. Biochem. 41:7008-7020.
                                         

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This image depicts a monomer of a Tau class GST isolated from wheat.  As observed in other GSTs, the N-terminal domain forms a beta-alpha-beta element connected to a beta-beta-alpha element by an alpha helical section that is exposed to solvent
 
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