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1gnw

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[[Image:1gnw.gif|left|200px]]
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{{STRUCTURE_1gnw| PDB=1gnw | SCENE= }}
{{STRUCTURE_1gnw| PDB=1gnw | SCENE= }}
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'''STRUCTURE OF GLUTATHIONE S-TRANSFERASE'''
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===STRUCTURE OF GLUTATHIONE S-TRANSFERASE===
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==Overview==
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Glutathione S-transferases (GST) are a family of multifunctional enzymes involved in the metabolization of a broad variety of xenobiotics and reactive endogenous compounds. The interest in plant glutathione S-transferases may be attributed to their agronomic value, since it has been demonstrated that glutathione conjugation for a variety of herbicides is the major resistance and selectivity factor in plants. The three-dimensional structure of glutathione S-transferase from the plant Arabidopsis thaliana has been solved by multiple isomorphous replacement and multiwavelength anomalous dispersion techniques at 3 A resolution and refined to a final crystallographic R-factor of 17.5% using data from 8 to 2.2 A resolution. The enzyme forms a dimer of two identical subunits each consisting of 211 residues. Each subunit is characterized by the GST-typical modular structure with two spatially distinct domains. Domain I consists of a central four-stranded beta-sheet flanked on one side by two alpha-helices and on the other side by an irregular segment containing three short 3(10)-helices, while domain II is entirely helical. The dimeric molecule is globular with a prominent large cavity formed between the two subunits. The active site is located in a cleft situated between domains I and II and each subunit binds two molecules of a competitive inhibitor S-hexylglutathione. Both hexyl moieties are oriented parallel and fill the H-subsite of the enzyme's active site. The glutathione peptide of one inhibitor, termed productive binding, occupies the G-subsite with multiple interactions similar to those observed for other glutathione S-transferases, while the glutathione backbone of the second inhibitor, termed unproductive binding, exhibits only weak interactions mediated by two polar contacts. A most striking difference from the mammalian glutathione S-transferases, which share a conserved catalytic tyrosine residue, is the lack of this tyrosine in the active site of the plant glutathione S-transferase.
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(as it appears on PubMed at http://www.pubmed.gov), where 8551521 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8551521}}
==About this Structure==
==About this Structure==
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[[Category: Herbicide detoxification]]
[[Category: Herbicide detoxification]]
[[Category: Transferase]]
[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 05:34:55 2008''

Revision as of 02:34, 1 July 2008

Image:1gnw.png

Template:STRUCTURE 1gnw

STRUCTURE OF GLUTATHIONE S-TRANSFERASE

Template:ABSTRACT PUBMED 8551521

About this Structure

1GNW is a Single protein structure of sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA.

Reference

Three-dimensional structure of glutathione S-transferase from Arabidopsis thaliana at 2.2 A resolution: structural characterization of herbicide-conjugating plant glutathione S-transferases and a novel active site architecture., Reinemer P, Prade L, Hof P, Neuefeind T, Huber R, Zettl R, Palme K, Schell J, Koelln I, Bartunik HD, Bieseler B, J Mol Biol. 1996 Jan 19;255(2):289-309. PMID:8551521

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