1oyj

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[[Image:1oyj.jpg|left|200px]]<br /><applet load="1oyj" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1oyj.jpg|left|200px]]
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caption="1oyj, resolution 1.95&Aring;" />
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'''Crystal structure solution of Rice GST1 (OsGSTU1) in complex with glutathione.'''<br />
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{{Structure
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|PDB= 1oyj |SIZE=350|CAPTION= <scene name='initialview01'>1oyj</scene>, resolution 1.95&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GTT:GLUTATHIONE'>GTT</scene>, <scene name='pdbligand=GSW:D-GAMMA-GLUTAMYL-L-CYSTEINYLGLYCINE'>GSW</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|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]
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|GENE=
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}}
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'''Crystal structure solution of Rice GST1 (OsGSTU1) in complex with glutathione.'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1OYJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryza_sativa Oryza sativa] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=GTT:'>GTT</scene>, <scene name='pdbligand=GSW:'>GSW</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OYJ OCA].
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1OYJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Oryza_sativa Oryza sativa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OYJ OCA].
==Reference==
==Reference==
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Forced evolution of a herbicide detoxifying glutathione transferase., Dixon DP, McEwen AG, Lapthorn AJ, Edwards R, J Biol Chem. 2003 Jun 27;278(26):23930-5. Epub 2003 Apr 11. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12692133 12692133]
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Forced evolution of a herbicide detoxifying glutathione transferase., Dixon DP, McEwen AG, Lapthorn AJ, Edwards R, J Biol Chem. 2003 Jun 27;278(26):23930-5. Epub 2003 Apr 11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12692133 12692133]
[[Category: Glutathione transferase]]
[[Category: Glutathione transferase]]
[[Category: Oryza sativa]]
[[Category: Oryza sativa]]
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[[Category: plant glutathione s-transferase]]
[[Category: plant glutathione s-transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:23:05 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:17:28 2008''

Revision as of 11:17, 20 March 2008


PDB ID 1oyj

Drag the structure with the mouse to rotate
, resolution 1.95Å
Ligands: , , , and
Activity: Glutathione transferase, with EC number 2.5.1.18
Coordinates: save as pdb, mmCIF, xml



Crystal structure solution of Rice GST1 (OsGSTU1) in complex with glutathione.


Overview

Plant Tau class glutathione transferases (GSTUs) detoxify diphenylether herbicides such as fluorodifen, determining their selectivity in crops and weeds. Using reconstructive PCR, a series of mutant GSTUs were generated from in vitro recombination and mutagenesis of the maize sequences ZmGSTU1 and ZmGSTU2 (with the prefix Zm designating Zea mays L.). A screen of 5000 mutant GSTUs identified seven enzymes with enhanced fluorodifen detoxifying activity. The best performing enhanced fluorodifen detoxifying mutant (EFD) had activity 19-fold higher than the parent enzymes, with a single point mutation conferring this enhancement. Further mutagenesis of this residue generated an EFD with a 29-fold higher catalytic efficiency toward fluorodifen as compared with the parents but with unaltered catalysis toward other substrates. When expressed in Arabidopsis thaliana, the optimized EFD, but not the parent enzymes, conferred enhanced tolerance to fluorodifen. Molecular modeling predicts that the serendipitous mutation giving the improvement in detoxification is due to the removal of an unfavorable interaction together with the introduction of a favorable change in conformation of residues 107-119, which contribute to herbicide binding.

About this Structure

1OYJ is a Single protein structure of sequence from Oryza sativa. Full crystallographic information is available from OCA.

Reference

Forced evolution of a herbicide detoxifying glutathione transferase., Dixon DP, McEwen AG, Lapthorn AJ, Edwards R, J Biol Chem. 2003 Jun 27;278(26):23930-5. Epub 2003 Apr 11. PMID:12692133

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