12gs

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(New page: 200px<br /> <applet load="12gs" size="450" color="white" frame="true" align="right" spinBox="true" caption="12gs, resolution 2.10&Aring;" /> '''GLUTATHIONE S-TRANS...)
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[[Image:12gs.gif|left|200px]]<br />
 
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<applet load="12gs" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="12gs, resolution 2.10&Aring;" />
 
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'''GLUTATHIONE S-TRANSFERASE COMPLEXED WITH S-NONYL-GLUTATHIONE'''<br />
 
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==Overview==
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==GLUTATHIONE S-TRANSFERASE COMPLEXED WITH S-NONYL-GLUTATHIONE==
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Glutathione S -transferases (GSTs) play a pivotal role in the, detoxification of foreign chemicals and toxic metabolites. They were, originally termed ligandins because of their ability to bind large, molecules (molecular masses &gt;400 Da), possibly for storage and transport, roles. The location of the ligandin site in mammalian GSTs is still, uncertain despite numerous studies in recent years. Here we show by X-ray, crystallography that the ligandin binding site in human pi class GST P1-1, occupies part of one of the substrate binding sites. This work has been, extended to the determination of a number of enzyme complex crystal, structures which show that very large ligands are readily accommodated, into this substrate binding site and in all, but one case, causes no, significant movement of protein side-chains. Some of these molecules make, use of a hitherto undescribed binding site located in a surface pocket of, the enzyme. This site is conserved in most, but not all, classes of GSTs, suggesting it may play an important functional role.
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<StructureSection load='12gs' size='340' side='right'caption='[[12gs]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[12gs]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=12GS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=12GS 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]] 2.1&#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=0HH:L-GAMMA-GLUTAMYL-S-NONYL-L-CYSTEINYLGLYCINE'>0HH</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</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=12gs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=12gs OCA], [https://pdbe.org/12gs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=12gs RCSB], [https://www.ebi.ac.uk/pdbsum/12gs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=12gs ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GSTP1_HUMAN GSTP1_HUMAN] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Regulates negatively CDK5 activity via p25/p35 translocation to prevent neurodegeneration.<ref>PMID:21668448</ref>
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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/2g/12gs_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=12gs ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Glutathione S -transferases (GSTs) play a pivotal role in the detoxification of foreign chemicals and toxic metabolites. They were originally termed ligandins because of their ability to bind large molecules (molecular masses &gt;400 Da), possibly for storage and transport roles. The location of the ligandin site in mammalian GSTs is still uncertain despite numerous studies in recent years. Here we show by X-ray crystallography that the ligandin binding site in human pi class GST P1-1 occupies part of one of the substrate binding sites. This work has been extended to the determination of a number of enzyme complex crystal structures which show that very large ligands are readily accommodated into this substrate binding site and in all, but one case, causes no significant movement of protein side-chains. Some of these molecules make use of a hitherto undescribed binding site located in a surface pocket of the enzyme. This site is conserved in most, but not all, classes of GSTs suggesting it may play an important functional role.
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==About this Structure==
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The ligandin (non-substrate) binding site of human Pi class glutathione transferase is located in the electrophile binding site (H-site).,Oakley AJ, Lo Bello M, Nuccetelli M, Mazzetti AP, Parker MW J Mol Biol. 1999 Aug 27;291(4):913-26. PMID:10452896<ref>PMID:10452896</ref>
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12GS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MES 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=12GS OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The ligandin (non-substrate) binding site of human Pi class glutathione transferase is located in the electrophile binding site (H-site)., Oakley AJ, Lo Bello M, Nuccetelli M, Mazzetti AP, Parker MW, J Mol Biol. 1999 Aug 27;291(4):913-26. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10452896 10452896]
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</div>
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[[Category: Glutathione transferase]]
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<div class="pdbe-citations 12gs" style="background-color:#fffaf0;"></div>
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[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Bello, M.Lo.]]
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[[Category: Oakley, A.J.]]
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[[Category: Parker, M.W.]]
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[[Category: MES]]
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[[Category: complex (transferase/nonyl-glutathione)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 15:52:54 2007''
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==See Also==
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*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Lo Bello M]]
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[[Category: Oakley AJ]]
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[[Category: Parker MW]]

Current revision

GLUTATHIONE S-TRANSFERASE COMPLEXED WITH S-NONYL-GLUTATHIONE

PDB ID 12gs

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