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New page: left|200px<br /><applet load="1gnw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gnw, resolution 2.2Å" /> '''STRUCTURE OF GLUTATHI...
 
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[[Image:1gnw.gif|left|200px]]<br /><applet load="1gnw" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1gnw, resolution 2.2&Aring;" />
'''STRUCTURE OF GLUTATHIONE S-TRANSFERASE'''<br />


==Overview==
==STRUCTURE OF GLUTATHIONE S-TRANSFERASE==
Glutathione S-transferases (GST) are a family of multifunctional enzymes, involved in the metabolization of a broad variety of xenobiotics and, reactive endogenous compounds. The interest in plant glutathione, S-transferases may be attributed to their agronomic value, since it has, been demonstrated that glutathione conjugation for a variety of herbicides, is the major resistance and selectivity factor in plants. The, three-dimensional structure of glutathione S-transferase from the plant, Arabidopsis thaliana has been solved by multiple isomorphous replacement, and multiwavelength anomalous dispersion techniques at 3 A resolution and, refined to a final crystallographic R-factor of 17.5% using data from 8 to, 2.2 A resolution. The enzyme forms a dimer of two identical subunits each, consisting of 211 residues. Each subunit is characterized by the, GST-typical modular structure with two spatially distinct domains. Domain, I consists of a central four-stranded beta-sheet flanked on one side by, two alpha-helices and on the other side by an irregular segment containing, three short 3(10)-helices, while domain II is entirely helical. The, dimeric molecule is globular with a prominent large cavity formed between, the two subunits. The active site is located in a cleft situated between, domains I and II and each subunit binds two molecules of a competitive, inhibitor S-hexylglutathione. Both hexyl moieties are oriented parallel, and fill the H-subsite of the enzyme's active site. The glutathione, peptide of one inhibitor, termed productive binding, occupies the, G-subsite with multiple interactions similar to those observed for other, glutathione S-transferases, while the glutathione backbone of the second, inhibitor, termed unproductive binding, exhibits only weak interactions, mediated by two polar contacts. A most striking difference from the, mammalian glutathione S-transferases, which share a conserved catalytic, tyrosine residue, is the lack of this tyrosine in the active site of the, plant glutathione S-transferase.
<StructureSection load='1gnw' size='340' side='right'caption='[[1gnw]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1gnw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GNW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GNW FirstGlance]. <br>
</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>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTX:S-HEXYLGLUTATHIONE'>GTX</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gnw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gnw OCA], [https://pdbe.org/1gnw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gnw RCSB], [https://www.ebi.ac.uk/pdbsum/1gnw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gnw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GSTF2_ARATH GSTF2_ARATH] Binds auxin, endogenous flavonoids and the phytoalexin camalexin and may be involved in regulating the binding and transport of small bioactive natural products and defense-related compounds during plant stress. Binds a series of heterocyclic compounds, including lumichrome, harmane, norharmane and indole-3-aldehyde. In vitro, possesses glutathione S-transferase activity toward 1-chloro-2,4-dinitrobenzene (CDNB) and benzyl isothiocyanate (BITC). Acts as glutathione peroxidase on cumene hydroperoxide, linoleic acid-13-hydroperoxide and trans-stilbene oxide, but not trans-cinnamic acid or IAA-CoA.<ref>PMID:12090627</ref> <ref>PMID:21631432</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gn/1gnw_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1gnw ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1GNW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] with GTX as [http://en.wikipedia.org/wiki/ligand ligand]. 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GNW OCA].
*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
 
== References ==
==Reference==
<references/>
Three-dimensional structure of glutathione S-transferase from Arabidopsis thaliana at 2.2 A resolution: structural characterization of herbicide-conjugating plant glutathione S-transferases and a novel active site architecture., Reinemer P, Prade L, Hof P, Neuefeind T, Huber R, Zettl R, Palme K, Schell J, Koelln I, Bartunik HD, Bieseler B, J Mol Biol. 1996 Jan 19;255(2):289-309. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8551521 8551521]
__TOC__
</StructureSection>
[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
[[Category: Glutathione transferase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Bartunik HD]]
[[Category: Bartunik, H.D.]]
[[Category: Bieseler B]]
[[Category: Bieseler, B.]]
[[Category: Hof P]]
[[Category: Hof, P.]]
[[Category: Huber R]]
[[Category: Huber, R.]]
[[Category: Neuefeind T]]
[[Category: Neuefeind, T.]]
[[Category: Palme K]]
[[Category: Palme, K.]]
[[Category: Prade L]]
[[Category: Prade, L.]]
[[Category: Reinemer P]]
[[Category: Reinemer, P.]]
[[Category: GTX]]
[[Category: herbicide detoxification]]
[[Category: transferase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:11:34 2007''

Latest revision as of 07:25, 7 February 2024

STRUCTURE OF GLUTATHIONE S-TRANSFERASE

1gnw, resolution 2.20Å

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