1aw9

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[[Image:1aw9.png|left|200px]]
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==STRUCTURE OF GLUTATHIONE S-TRANSFERASE III IN APO FORM==
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<StructureSection load='1aw9' size='340' side='right' caption='[[1aw9]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1aw9]] is a 1 chain structure with 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=1AW9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AW9 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene><br>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1aw9 RCSB], [http://www.ebi.ac.uk/pdbsum/1aw9 PDBsum]</span></td></tr>
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<table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/aw/1aw9_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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{{STRUCTURE_1aw9| PDB=1aw9 | SCENE= }}
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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<ref>PMID:9417936</ref>
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===STRUCTURE OF GLUTATHIONE S-TRANSFERASE III IN APO FORM===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_9417936}}
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==See Also==
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*[[Glutathione S-transferase|Glutathione S-transferase]]
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==About this Structure==
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== References ==
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[[1aw9]] is a 1 chain structure with 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=1AW9 OCA].
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<references/>
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__TOC__
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==Reference==
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</StructureSection>
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<ref group="xtra">PMID:009417936</ref><references group="xtra"/>
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[[Category: Glutathione transferase]]
[[Category: Glutathione transferase]]
[[Category: Zea mays]]
[[Category: Zea mays]]

Revision as of 08:07, 30 July 2014

STRUCTURE OF GLUTATHIONE S-TRANSFERASE III IN APO FORM

1aw9, resolution 2.20Å

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