1axd
From Proteopedia
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|PDB= 1axd |SIZE=350|CAPTION= <scene name='initialview01'>1axd</scene>, resolution 2.5Å | |PDB= 1axd |SIZE=350|CAPTION= <scene name='initialview01'>1axd</scene>, resolution 2.5Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=LAC:LACTIC ACID'>LAC</scene> | + | |LIGAND= <scene name='pdbligand=LAC:LACTIC+ACID'>LAC</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1axd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1axd OCA], [http://www.ebi.ac.uk/pdbsum/1axd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1axd RCSB]</span> | ||
}} | }} | ||
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[[Category: Neuefeind, T.]] | [[Category: Neuefeind, T.]] | ||
[[Category: Prade, L.]] | [[Category: Prade, L.]] | ||
| - | [[Category: LAC]] | ||
[[Category: complex (transferase/ligand)]] | [[Category: complex (transferase/ligand)]] | ||
[[Category: herbicide detoxification]] | [[Category: herbicide detoxification]] | ||
[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:49:20 2008'' |
Revision as of 15:49, 30 March 2008
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| , resolution 2.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Glutathione transferase, with EC number 2.5.1.18 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF GLUTATHIONE S-TRANSFERASE-I BOUND WITH THE LIGAND LACTOYLGLUTATHIONE
Overview
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.
About this Structure
1AXD is a Single protein structure of sequence from Zea mays. Full crystallographic information is available from OCA.
Reference
Crystal structure of herbicide-detoxifying maize glutathione S-transferase-I in complex with lactoylglutathione: evidence for an induced-fit mechanism., Neuefeind T, Huber R, Dasenbrock H, Prade L, Bieseler B, J Mol Biol. 1997 Dec 12;274(4):446-53. PMID:9417926
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