1ev4

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(New page: 200px<br /><applet load="1ev4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ev4, resolution 2.2&Aring;" /> '''RAT GLUTATHIONE S-TRA...)
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[[Image:1ev4.jpg|left|200px]]<br /><applet load="1ev4" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ev4, resolution 2.2&Aring;" />
 
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'''RAT GLUTATHIONE S-TRANSFERASE A1-1: MUTANT W21F/F220Y WITH GSO3 BOUND'''<br />
 
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==Overview==
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==RAT GLUTATHIONE S-TRANSFERASE A1-1: MUTANT W21F/F220Y WITH GSO3 BOUND==
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Twelve C-terminal residues of human glutathione S-transferase A1-1 form a, helix in the presence of glutathione-conjugate, or substrate alone, and, partly cover the active site. According to X-ray structures, the helix is, disordered in the absence of glutathione, but it is not known if it is, helical and delocalized, or in a random-coil conformation. Mutation to a, tyrosine of residue 220 within this helix was previously shown to affect, the pK(a) of Tyr-9 at the active site, in the apo form of the enzyme, and, it was proposed that an on-face hydrogen bond between Tyr-220 and Tyr-9, provided a means for affecting this pK(a). In the current study, X-ray, structures of the W21F and of the C-terminal mutation, W21F/F220Y, with, glutathione sulfonate bound, show that the C-terminal helix is disordered, (or delocalized) in the W21F crystal but is visible and ordered in a novel, location, a crystal packing crevice, in one of three monomers in the, W21F/F220Y crystal, and the proposed hydrogen bond is not formed., Fluorescence spectroscopy studies using an engineered F222W mutant show, that the C-terminus remains delocalized in the absence of glutathione or, when only the glutathione binding site is occupied, but is ordered and, localized in the presence of substrate or conjugate, consistent with these, and previous crystallographic studies. Proteins 2001;42:192-200.
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<StructureSection load='1ev4' size='340' side='right'caption='[[1ev4]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ev4]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EV4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EV4 FirstGlance]. <br>
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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]] 2.2&#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=GTS:GLUTATHIONE+SULFONIC+ACID'>GTS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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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=1ev4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ev4 OCA], [https://pdbe.org/1ev4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ev4 RCSB], [https://www.ebi.ac.uk/pdbsum/1ev4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ev4 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GSTA1_RAT GSTA1_RAT] 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/ev/1ev4_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=1ev4 ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1EV4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with SO4 and GTS as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1EV4 OCA].
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*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Localization of the C-terminus of rat glutathione S-transferase A1-1: crystal structure of mutants W21F and W21F/F220Y., Adman ET, Le Trong I, Stenkamp RE, Nieslanik BS, Dietze EC, Tai G, Ibarra C, Atkins WM, Proteins. 2001 Feb 1;42(2):192-200. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11119643 11119643]
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[[Category: Large Structures]]
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[[Category: Glutathione transferase]]
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Single protein]]
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[[Category: Adman ET]]
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[[Category: Adman, E.T.]]
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[[Category: Atkins WM]]
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[[Category: Atkins, W.M.]]
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[[Category: Dietze EC]]
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[[Category: Dietze, E.C.]]
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[[Category: Ibarra C]]
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[[Category: Ibarra, C.]]
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[[Category: Le Trong I]]
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[[Category: Nieslanik, B.S.]]
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[[Category: Nieslanik BS]]
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[[Category: Stenkamp, R.E.]]
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[[Category: Stenkamp RE]]
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[[Category: Tai, G.]]
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[[Category: Tai G]]
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[[Category: Trong, I.Le.]]
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[[Category: GTS]]
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[[Category: SO4]]
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[[Category: disordered c-terminal helices]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:20:35 2007''
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Current revision

RAT GLUTATHIONE S-TRANSFERASE A1-1: MUTANT W21F/F220Y WITH GSO3 BOUND

PDB ID 1ev4

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