1aw9

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[[Image:1aw9.gif|left|200px]]
[[Image:1aw9.gif|left|200px]]
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{{Structure
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|PDB= 1aw9 |SIZE=350|CAPTION= <scene name='initialview01'>1aw9</scene>, resolution 2.2&Aring;
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The line below this paragraph, containing "STRUCTURE_1aw9", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|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>
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{{STRUCTURE_1aw9| PDB=1aw9 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1aw9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aw9 OCA], [http://www.ebi.ac.uk/pdbsum/1aw9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1aw9 RCSB]</span>
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'''STRUCTURE OF GLUTATHIONE S-TRANSFERASE III IN APO FORM'''
'''STRUCTURE OF GLUTATHIONE S-TRANSFERASE III IN APO FORM'''
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[[Category: Neuefeind, T.]]
[[Category: Neuefeind, T.]]
[[Category: Reinemer, P.]]
[[Category: Reinemer, P.]]
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[[Category: herbicide detoxification]]
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[[Category: Herbicide detoxification]]
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[[Category: transferase]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:46:20 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:48:44 2008''
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Revision as of 07:46, 2 May 2008

Image:1aw9.gif

Template:STRUCTURE 1aw9

STRUCTURE OF GLUTATHIONE S-TRANSFERASE III IN APO FORM


Overview

Glutathione S-transferases (GSTs) are enzymes that inactivate toxic compounds by conjugation with glutathione and are involved in resistance towards drugs, antibiotics, insecticides and herbicides. Their ability to confer herbicide tolerance in plants provides a tool to control weeds in a wide variety of agronomic crops. GST-III was prepared from Zea mays var. mutin and its amino acid sequence was determined from two sets of peptides obtained by cleavage with endoprotease Asp-N and with trypsin, respectively. Recombinant GST-III was prepared by extraction of mRNA from plant tissue, transcription into cDNA, amplification by PCR and expression. It was crystallized and the crystal structure of the unligated form was determined at 2.2 A resolution. The enzyme forms a GST-typical dimer with one subunit consisting of 220 residues. Each subunit is formed of two distinct domains, an N-terminal domain consisting of a beta-sheet flanked by two helices, and a C-terminal domain, entirely helical. The dimeric molecule is globular with a large cleft between the two subunits. The amino acid sequence of GST-III and its cDNA sequence determined here show differences from sequences published earlier.

About this Structure

1AW9 is a Single protein structure of sequence from Zea mays. Full crystallographic information is available from OCA.

Reference

Cloning, sequencing, crystallization and X-ray structure of glutathione S-transferase-III from Zea mays var. mutin: a leading enzyme in detoxification of maize herbicides., Neuefeind T, Huber R, Reinemer P, Knablein J, Prade L, Mann K, Bieseler B, J Mol Biol. 1997 Dec 12;274(4):577-87. PMID:9417936 Page seeded by OCA on Fri May 2 10:46:20 2008

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