1aw9

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[[Image:1aw9.gif|left|200px]]
 
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==STRUCTURE OF GLUTATHIONE S-TRANSFERASE III IN APO FORM==
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The line below this paragraph, containing "STRUCTURE_1aw9", creates the "Structure Box" on the page.
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<StructureSection load='1aw9' size='340' side='right'caption='[[1aw9]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1aw9]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=1AW9 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></td></tr>
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{{STRUCTURE_1aw9| PDB=1aw9 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1aw9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aw9 OCA], [https://pdbe.org/1aw9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aw9 RCSB], [https://www.ebi.ac.uk/pdbsum/1aw9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aw9 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q9ZP62_MAIZE Q9ZP62_MAIZE]
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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/main_output.php?pdb_ID=1aw9 ConSurf].
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<div style="clear:both"></div>
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'''STRUCTURE OF GLUTATHIONE S-TRANSFERASE III IN APO FORM'''
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==See Also==
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*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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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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[[Category: Large Structures]]
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==About this Structure==
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1AW9 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=1AW9 OCA].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/9417936 9417936]
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[[Category: Glutathione transferase]]
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[[Category: Single protein]]
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[[Category: Zea mays]]
[[Category: Zea mays]]
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[[Category: Huber, R.]]
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[[Category: Huber R]]
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[[Category: Knaeblein, J.]]
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[[Category: Knaeblein J]]
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[[Category: Neuefeind, T.]]
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[[Category: Neuefeind T]]
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[[Category: Reinemer, P.]]
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[[Category: Reinemer P]]
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[[Category: Herbicide detoxification]]
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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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Current revision

STRUCTURE OF GLUTATHIONE S-TRANSFERASE III IN APO FORM

PDB ID 1aw9

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