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New page: left|200px<br /><applet load="1gsu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gsu, resolution 1.94Å" /> '''AN AVIAN CLASS-MU GL...
 
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[[Image:1gsu.gif|left|200px]]<br /><applet load="1gsu" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1gsu, resolution 1.94&Aring;" />
'''AN AVIAN CLASS-MU GLUTATHIONE S-TRANSFERASE, CGSTM1-1 AT 1.94 ANGSTROM RESOLUTION'''<br />


==Overview==
==AN AVIAN CLASS-MU GLUTATHIONE S-TRANSFERASE, CGSTM1-1 AT 1.94 ANGSTROM RESOLUTION==
Glutathione S-transferase cGSTM1-1, an avian class-mu enzyme with high, sequence identity with rGSTM3-3, was expressed heterologously in, Escherichia coli. The three-dimensional structure of this protein that, co-crystallized with an inhibitor, S-hexylglutathione, was determined by, the molecular replacement method and refined to 1.94 A resolution. The, three-dimensional structure and the folding topology of the dimeric, cGSTM1-1 closely resembles those of other class-mu GSTs. The bound, inhibitor, S-hexylglutathione, orients in disparate directions in the two, subunits. The combined space occupied by the hexyl moiety of the, inhibitors overlaps with that reported for rGSTM1-1 co-crystallized with, (9 S,10 S)-9-(S-glutathionyl)-10-hydroxy-9,10-dihydrophenanthrene., Conformational differences at a flexible loop (residue 35 to 40) were also, observed between the crystal structures of cGSTM1-1 and rGSTM1-1.cGSTM1-1, has the highest epoxidase activity among all the class-mu enzymes, reported. Tyr115, has been identified as a residue that participates in, the epoxidase activity of class-mu glutathione S-transferase and is, conserved in cGSTM1-1. The epoxidase and trans-4-phenyl-3-buten-2-one, conjugating activity of cGSTM1-1 are decreased drastically but not, abolished by replacing Tyr115 with phenylalanine. The specificity constant, of the cGSTM1-1(Y115F) mutant, with 1-chloro-2,4-dinitrobenzene as, substrate, is 15-fold higher than that of the wild-type enzyme.
<StructureSection load='1gsu' size='340' side='right'caption='[[1gsu]], [[Resolution|resolution]] 1.94&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1gsu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GSU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GSU 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]] 1.94&#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=1gsu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gsu OCA], [https://pdbe.org/1gsu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gsu RCSB], [https://www.ebi.ac.uk/pdbsum/1gsu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gsu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GSTM2_CHICK GSTM2_CHICK] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
== 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/gs/1gsu_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=1gsu ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1GSU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] 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=1GSU OCA].
*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
The three-dimensional structure of an avian class-mu glutathione S-transferase, cGSTM1-1 at 1.94 A resolution., Sun YJ, Kuan IC, Tam MF, Hsiao CD, J Mol Biol. 1998 Apr 24;278(1):239-52. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9571047 9571047]
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Glutathione transferase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Hsiao C-D]]
[[Category: Hsiao, C.D.]]
[[Category: Kuan C]]
[[Category: Kuan, C.]]
[[Category: Sun Y-J]]
[[Category: Sun, Y.J.]]
[[Category: Tam MF]]
[[Category: Tam, M.F.]]
[[Category: GTX]]
[[Category: detoxification enzyme]]
[[Category: glutathione s-transferase]]
[[Category: s-hexyl glutathione]]
 
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