1gwc
From Proteopedia
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THE STRUCTURE OF A TAU CLASS GLUTATHIONE S-TRANSFERASE FROM WHEAT, ACTIVE IN HERBICIDE DETOXIFICATION
Overview
Glutathione S-transferases (GSTs) from the phi (GSTF) and tau (GSTU), classes are unique to plants and play important roles in stress tolerance, and secondary metabolism as well as catalyzing the detoxification of, herbicides in crops and weeds. We have cloned and functionally, characterized a group of GSTUs from wheat treated with, fenchlorazole-ethyl, a herbicide safener. One of these enzymes, TaGSTU4-4, was highly active in conjugating the chemically distinct wheat herbicides, fenoxaprop and dimethenamid. The structure of TaGSTU4-4 has been, determined at 2.2 A resolution in complex with S-hexylglutathione. This, enzyme is the first tau class GST structure to be determined and most, closely resembles the omega class GSTs, but without the unique N-terminal, extension or active site cysteine. The X-ray structure identifies key, amino acid residues in the hydrophobic binding site and provides insights, into the substrate specificity of these enzymes.
About this Structure
1GWC is a Single protein structure of sequence from Aegilops tauschii with SO4 and GTX as ligands. Active as Glutathione transferase, with EC number 2.5.1.18 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Structure of a tau class glutathione S-transferase from wheat active in herbicide detoxification., Thom R, Cummins I, Dixon DP, Edwards R, Cole DJ, Lapthorn AJ, Biochemistry. 2002 Jun 4;41(22):7008-20. PMID:12033934
Page seeded by OCA on Tue Dec 18 15:41:35 2007
