1oyj
From Proteopedia
(New page: 200px<br /><applet load="1oyj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oyj, resolution 1.95Å" /> '''Crystal structure so...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1oyj.jpg|left|200px]]<br /><applet load="1oyj" size=" | + | [[Image:1oyj.jpg|left|200px]]<br /><applet load="1oyj" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1oyj, resolution 1.95Å" /> | caption="1oyj, resolution 1.95Å" /> | ||
'''Crystal structure solution of Rice GST1 (OsGSTU1) in complex with glutathione.'''<br /> | '''Crystal structure solution of Rice GST1 (OsGSTU1) in complex with glutathione.'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Plant Tau class glutathione transferases (GSTUs) detoxify diphenylether | + | 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== | ==About this Structure== | ||
| - | 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 MG, CL, GTT, GSW and GOL 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:// | + | 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]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Oryza sativa]] | [[Category: Oryza sativa]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Dixon, D | + | [[Category: Dixon, D P.]] |
[[Category: Edwards, R.]] | [[Category: Edwards, R.]] | ||
| - | [[Category: Lapthorn, A | + | [[Category: Lapthorn, A J.]] |
| - | [[Category: McEwen, A | + | [[Category: McEwen, A G.]] |
[[Category: CL]] | [[Category: CL]] | ||
[[Category: GOL]] | [[Category: GOL]] | ||
| Line 26: | Line 26: | ||
[[Category: plant glutathione s-transferase]] | [[Category: plant glutathione s-transferase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:23:05 2008'' |
Revision as of 12:23, 21 February 2008
|
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 with , , , and as ligands. Active as Glutathione transferase, with EC number 2.5.1.18 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
Page seeded by OCA on Thu Feb 21 14:23:05 2008
