1bye
From Proteopedia
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| - | [[Image:1bye.gif|left|200px]] | + | [[Image:1bye.gif|left|200px]] |
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| - | '''GLUTATHIONE S-TRANSFERASE I FROM MAIS IN COMPLEX WITH ATRAZINE GLUTATHIONE CONJUGATE''' | + | {{Structure |
| + | |PDB= 1bye |SIZE=350|CAPTION= <scene name='initialview01'>1bye</scene>, resolution 2.80Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ATA:ATRAZINE GLUTATHIONE CONJUGATE'>ATA</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''GLUTATHIONE S-TRANSFERASE I FROM MAIS IN COMPLEX WITH ATRAZINE GLUTATHIONE CONJUGATE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1BYE is a [ | + | 1BYE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Zea_mays Zea mays]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BYE OCA]. |
==Reference== | ==Reference== | ||
| - | Structures of herbicides in complex with their detoxifying enzyme glutathione S-transferase - explanations for the selectivity of the enzyme in plants., Prade L, Huber R, Bieseler B, Structure. 1998 Nov 15;6(11):1445-52. PMID:[http:// | + | Structures of herbicides in complex with their detoxifying enzyme glutathione S-transferase - explanations for the selectivity of the enzyme in plants., Prade L, Huber R, Bieseler B, Structure. 1998 Nov 15;6(11):1445-52. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9817846 9817846] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Zea mays]] | [[Category: Zea mays]] | ||
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[[Category: herbicide]] | [[Category: herbicide]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:17:26 2008'' |
Revision as of 08:17, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
GLUTATHIONE S-TRANSFERASE I FROM MAIS IN COMPLEX WITH ATRAZINE GLUTATHIONE CONJUGATE
Overview
BACKGROUND: Glutathione S-transferases (GSTs) are detoxifying enzymes present in all aerobic organisms. These enzymes catalyse the conjugation of glutathione with a variety of electrophilic compounds. In plants, GSTs catalyse the first step in the degradation of several herbicides, such as triazines and acetamides, thus playing an important role in herbicide tolerance. RESULTS: We have solved the structures of GST-I from maize in complex with an atrazine-glutathione conjugate (at 2.8 A resolution) and GST from Arabidopsis thaliana (araGST) in complex with an FOE-4053-glutathione conjugate (at 2.6 A resolution). These ligands are products of the detoxifying reaction and are well defined in the electron density. The herbicide-binding site (H site) is different in the two structures. The architecture of the glutathione-binding site (G site) of araGST is different to that of the previously described structure of GST in complex with two S-hexylglutathione molecules, but is homologous to that of GST-I. CONCLUSIONS: Three features are responsible for the differences in the H site of the two GSTs described here: the exchange of hydrophobic residues of different degrees of bulkiness; a slight difference in the location of the H site; and a difference in the degree of flexibility of the upper side of the H site, which is built up by the loop between helices alpha4 and alpha5. Taking these two structures as a model, the different substrate specificities of other plant GSTs may be explained. The structures reported here provide a basis for the design of new, more selective herbicides.
About this Structure
1BYE is a Single protein structure of sequence from Zea mays. Full crystallographic information is available from OCA.
Reference
Structures of herbicides in complex with their detoxifying enzyme glutathione S-transferase - explanations for the selectivity of the enzyme in plants., Prade L, Huber R, Bieseler B, Structure. 1998 Nov 15;6(11):1445-52. PMID:9817846
Page seeded by OCA on Thu Mar 20 10:17:26 2008
