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1gsu

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[[Image:1gsu.gif|left|200px]]
 
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==AN AVIAN CLASS-MU GLUTATHIONE S-TRANSFERASE, CGSTM1-1 AT 1.94 ANGSTROM RESOLUTION==
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The line below this paragraph, containing "STRUCTURE_1gsu", creates the "Structure Box" on the page.
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<StructureSection load='1gsu' size='340' side='right'caption='[[1gsu]], [[Resolution|resolution]] 1.94&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'>[[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>
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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]] 1.94&#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=GTX:S-HEXYLGLUTATHIONE'>GTX</scene></td></tr>
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{{STRUCTURE_1gsu| PDB=1gsu | 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=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>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GSTM2_CHICK GSTM2_CHICK] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
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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/gs/1gsu_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=1gsu ConSurf].
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<div style="clear:both"></div>
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'''AN AVIAN CLASS-MU GLUTATHIONE S-TRANSFERASE, CGSTM1-1 AT 1.94 ANGSTROM RESOLUTION'''
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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-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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==About this Structure==
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1GSU is a [[Single protein]] structure of sequence from [http://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].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/9571047 9571047]
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[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
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[[Category: Glutathione transferase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Hsiao C-D]]
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[[Category: Hsiao, C D.]]
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[[Category: Kuan C]]
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[[Category: Kuan, C.]]
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[[Category: Sun Y-J]]
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[[Category: Sun, Y J.]]
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[[Category: Tam MF]]
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[[Category: Tam, M F.]]
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[[Category: Detoxification enzyme]]
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[[Category: Glutathione s-transferase]]
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[[Category: S-hexyl glutathione]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:57:54 2008''
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Current revision

AN AVIAN CLASS-MU GLUTATHIONE S-TRANSFERASE, CGSTM1-1 AT 1.94 ANGSTROM RESOLUTION

PDB ID 1gsu

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