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| <StructureSection load='1gsu' size='340' side='right'caption='[[1gsu]], [[Resolution|resolution]] 1.94Å' scene=''> | | <StructureSection load='1gsu' size='340' side='right'caption='[[1gsu]], [[Resolution|resolution]] 1.94Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[1gsu]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Chick Chick]. 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 [http://proteopedia.org/fgij/fg.htm?mol=1GSU FirstGlance]. <br> | | <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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTX:S-HEXYLGLUTATHIONE'>GTX</scene></td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.94Å</td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CGSTM1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 CHICK])</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='activity'><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>
| | <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> |
| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1gsu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gsu OCA], [http://pdbe.org/1gsu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gsu RCSB], [http://www.ebi.ac.uk/pdbsum/1gsu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1gsu ProSAT]</span></td></tr> | |
| </table> | | </table> |
| == Function == | | == Function == |
| [[http://www.uniprot.org/uniprot/GSTM2_CHICK GSTM2_CHICK]] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. | | [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 == | | == Evolutionary Conservation == |
| [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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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=1gsu ConSurf]. | | </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> | | <div style="clear:both"></div> |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| 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.
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| 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:9571047<ref>PMID:9571047</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 1gsu" style="background-color:#fffaf0;"></div>
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| ==See Also== | | ==See Also== |
| *[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]] | | *[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]] |
| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Chick]] | | [[Category: Gallus gallus]] |
| [[Category: Glutathione transferase]]
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| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Hsiao, C D]] | | [[Category: Hsiao C-D]] |
| [[Category: Kuan, C]] | | [[Category: Kuan C]] |
| [[Category: Sun, Y J]] | | [[Category: Sun Y-J]] |
| [[Category: Tam, M F]] | | [[Category: Tam MF]] |
| [[Category: Detoxification enzyme]]
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| [[Category: Glutathione s-transferase]]
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| [[Category: S-hexyl glutathione]]
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