1GNW

STRUCTURE OF GLUTATHIONE S-TRANSFERASE

Summary for 1GNW

• Entry DOI: 10.2210/pdb1gnw/pdb
• Descriptor: GLUTATHIONE S-TRANSFERASE, S-HEXYLGLUTATHIONE (3 entities in total)
• Functional Keywords: transferase, herbicide detoxification
• Biological source: Arabidopsis thaliana (thale cress)
• Cellular location: Cytoplasm, cytosol : P46422
• Total number of polymer chains: 2
• Total formula weight: 49632.71

Authors

Reinemer, P.,Prade, L.,Hof, P.,Neuefeind, T.,Huber, R.,Palme, K.,Bartunik, H.D.,Bieseler, B. (deposition date: 1996-09-15, release date: 1997-09-17, Last modification date: 2024-02-07)

Primary citation

Reinemer, P.,Prade, L.,Hof, P.,Neuefeind, T.,Huber, R.,Zettl, R.,Palme, K.,Schell, J.,Koelln, I.,Bartunik, H.D.,Bieseler, B.
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.
J.Mol.Biol., 255:289-309, 1996

PubMed Abstract: 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.

PubMed: 8551521
DOI: 10.1006/jmbi.1996.0024

Experimental method

X-RAY DIFFRACTION (2.2 Å)