This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1axd
From Proteopedia
| Line 4: | Line 4: | ||
|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> | ||
}} | }} | ||
| Line 28: | Line 31: | ||
[[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
| |||||||
| , 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
Page seeded by OCA on Sun Mar 30 18:49:20 2008
