View source for 1axd


==STRUCTURE OF GLUTATHIONE S-TRANSFERASE-I BOUND WITH THE LIGAND LACTOYLGLUTATHIONE==
<StructureSection load='1axd' size='340' side='right'caption='[[1axd]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1axd]] is a 4 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=1AXD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AXD 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]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CYW:S-[(2R)-2-HYDROXYPROPANOYL]-L-CYSTEINE'>CYW</scene>, <scene name='pdbligand=GGL:GAMMA-L-GLUTAMIC+ACID'>GGL</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=1axd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1axd OCA], [https://pdbe.org/1axd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1axd RCSB], [https://www.ebi.ac.uk/pdbsum/1axd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1axd ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GSTF1_MAIZE GSTF1_MAIZE] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Involved in the detoxification of certain herbicides.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
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    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ax/1axd_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=1axd ConSurf].
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== Publication Abstract from PubMed ==
Glutathione S-transferases (GSTs) -I and -III are involved in herbicide metabolism in maize and have been intensively studied. Starting with plant tissue from Zea mays var. mutin recombinant GST-I was prepared by heterologous expression in Escherichia coli. The enzyme was crystallized in the presence of lactoylglutathione, a ligand formerly never observed in a GST structure and known as an intermediate of the pharmacologically relevant glyoxalase system. The crystal structure of GST-I has been determined at 2.5 A resolution and exhibits the GST-typical dimer of two identical subunits, each consisting of 214 residues. Compared with other plant GSTs the three-dimensional structure of GST-I primarily shows structural differences in the hydrophobic substrate binding site, the linker segment and the C-terminal region. Furthermore, a comparison of the ligand-bound GST-I structure with the apo structure of GST-III indicates the movement of a ten-residue loop upon binding of the ligand to the active site. This is the first structure-based evidence for an induced fit mechanism of glutathione S-transferases, which has previously been postulated for class pi enzymes. Together with GST-III, GST-I may explain herbicide resistance and selectivity in maize as well as in other agronomic relevant crops.

Crystal structure of herbicide-detoxifying maize glutathione S-transferase-I in complex with lactoylglutathione: evidence for an induced-fit mechanism.,Neuefeind T, Huber R, Dasenbrock H, Prade L, Bieseler B J Mol Biol. 1997 Dec 12;274(4):446-53. PMID:9417926<ref>PMID:9417926</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Zea mays]]
[[Category: Bieseler B]]
[[Category: Dasenbrock H]]
[[Category: Huber R]]
[[Category: Neuefeind T]]
[[Category: Prade L]]