1aw9
From Proteopedia
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STRUCTURE OF GLUTATHIONE S-TRANSFERASE III IN APO FORM
Overview
Glutathione S-transferases (GSTs) are enzymes that inactivate toxic, compounds by conjugation with glutathione and are involved in resistance, towards drugs, antibiotics, insecticides and herbicides. Their ability to, confer herbicide tolerance in plants provides a tool to control weeds in a, wide variety of agronomic crops. GST-III was prepared from Zea mays var., mutin and its amino acid sequence was determined from two sets of peptides, obtained by cleavage with endoprotease Asp-N and with trypsin, respectively. Recombinant GST-III was prepared by extraction of mRNA from, plant tissue, transcription into cDNA, amplification by PCR and, expression. It was crystallized and the crystal structure of the unligated, form was determined at 2.2 A resolution. The enzyme forms a GST-typical, dimer with one subunit consisting of 220 residues. Each subunit is formed, of two distinct domains, an N-terminal domain consisting of a beta-sheet, flanked by two helices, and a C-terminal domain, entirely helical. The, dimeric molecule is globular with a large cleft between the two subunits., The amino acid sequence of GST-III and its cDNA sequence determined here, show differences from sequences published earlier.
About this Structure
1AW9 is a Single protein structure of sequence from Zea mays with CD as ligand. Active as Glutathione transferase, with EC number 2.5.1.18 Full crystallographic information is available from OCA.
Reference
Cloning, sequencing, crystallization and X-ray structure of glutathione S-transferase-III from Zea mays var. mutin: a leading enzyme in detoxification of maize herbicides., Neuefeind T, Huber R, Reinemer P, Knablein J, Prade L, Mann K, Bieseler B, J Mol Biol. 1997 Dec 12;274(4):577-87. PMID:9417936
Page seeded by OCA on Sat Nov 24 23:24:45 2007
