1axd: Difference between revisions

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[[Image:1axd.gif|left|200px]]
{{Seed}}
[[Image:1axd.png|left|200px]]


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{{STRUCTURE_1axd|  PDB=1axd  |  SCENE=  }}  
{{STRUCTURE_1axd|  PDB=1axd  |  SCENE=  }}  


'''STRUCTURE OF GLUTATHIONE S-TRANSFERASE-I BOUND WITH THE LIGAND LACTOYLGLUTATHIONE'''
===STRUCTURE OF GLUTATHIONE S-TRANSFERASE-I BOUND WITH THE LIGAND LACTOYLGLUTATHIONE===




==Overview==
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Glutathione S-transferases (GSTs) -I and -III are involved in herbicide metabolism in maize and have been intensively studied. Starting with plant tissue from Zea mays var. mutin recombinant GST-I was prepared by heterologous expression in Escherichia coli. The enzyme was crystallized in the presence of lactoylglutathione, a ligand formerly never observed in a GST structure and known as an intermediate of the pharmacologically relevant glyoxalase system. The crystal structure of GST-I has been determined at 2.5 A resolution and exhibits the GST-typical dimer of two identical subunits, each consisting of 214 residues. Compared with other plant GSTs the three-dimensional structure of GST-I primarily shows structural differences in the hydrophobic substrate binding site, the linker segment and the C-terminal region. Furthermore, a comparison of the ligand-bound GST-I structure with the apo structure of GST-III indicates the movement of a ten-residue loop upon binding of the ligand to the active site. This is the first structure-based evidence for an induced fit mechanism of glutathione S-transferases, which has previously been postulated for class pi enzymes. Together with GST-III, GST-I may explain herbicide resistance and selectivity in maize as well as in other agronomic relevant crops.
The line below this paragraph, {{ABSTRACT_PUBMED_9417926}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_9417926}}


==About this Structure==
==About this Structure==
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[[Category: Herbicide detoxification]]
[[Category: Herbicide detoxification]]
[[Category: Transferase]]
[[Category: Transferase]]
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