1AXD
STRUCTURE OF GLUTATHIONE S-TRANSFERASE-I BOUND WITH THE LIGAND LACTOYLGLUTATHIONE
Summary for 1AXD
| Entry DOI | 10.2210/pdb1axd/pdb |
| Descriptor | GLUTATHIONE S-TRANSFERASE I, LACTOYLGLUTATHIONE (3 entities in total) |
| Functional Keywords | transferase, herbicide detoxification, transferase-transferase inhibitor complex, transferase/transferase inhibitor |
| Biological source | Zea mays |
| Total number of polymer chains | 4 |
| Total formula weight | 47420.56 |
| Authors | Neuefeind, T.,Huber, R.,Dasenbrock, H.,Prade, L.,Bieseler, B. (deposition date: 1997-10-15, release date: 1998-10-28, Last modification date: 2023-11-15) |
| Primary citation | Neuefeind, T.,Huber, R.,Dasenbrock, H.,Prade, L.,Bieseler, B. Crystal structure of herbicide-detoxifying maize glutathione S-transferase-I in complex with lactoylglutathione: evidence for an induced-fit mechanism. J.Mol.Biol., 274:446-453, 1997 Cited by PubMed Abstract: 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. PubMed: 9417926DOI: 10.1006/jmbi.1997.1402 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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