PDBsum entry 1gnw

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Transferase PDB id
Protein chains
210 a.a. *
GTX ×4
Waters ×660
* Residue conservation analysis

References listed in PDB file
Key reference
Title 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.
Authors P.Reinemer, L.Prade, P.Hof, T.Neuefeind, R.Huber, R.Zettl, K.Palme, J.Schell, I.Koelln, H.D.Bartunik, B.Bieseler.
Ref. J Mol Biol, 1996, 255, 289-309. [DOI no: 10.1006/jmbi.1996.0024]
PubMed id 8551521
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.
Figure 9.
Figure 9. A schematic represen- tation of the binding of the gluta- thione peptid of the productively bound inhibitor to the G-subsite of A. thaliana glutathone S-trans- ferase's active site.
Figure 10.
Figure 10. Superimposition of A. thaliana and mammalian glutathione S-transferase monomers complexed with their ligands; red, A. thaliana glutathione S-transferase; black, pi class isoenzyme (pGSTPI-1); ble, mu class isoenzyme (rGSTM3-3); and reen, alpha class isoenzyme (hGSTAI-1).
The above figures are reprinted by permission from Elsevier: J Mol Biol (1996, 255, 289-309) copyright 1996.
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