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14gs

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[[Image:14gs.gif|left|200px]]
 
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{{Structure
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==GLUTATHIONE S-TRANSFERASE P1-1 APO FORM 1==
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|PDB= 14gs |SIZE=350|CAPTION= <scene name='initialview01'>14gs</scene>, resolution 2.80&Aring;
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<StructureSection load='14gs' size='340' side='right'caption='[[14gs]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>
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<table><tr><td colspan='2'>[[14gs]] 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=14GS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=14GS FirstGlance]. <br>
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|ACTIVITY= <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>
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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]] 2.8&#8491;</td></tr>
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|GENE= GSTP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></td></tr>
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|DOMAIN=
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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=14gs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=14gs OCA], [https://pdbe.org/14gs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=14gs RCSB], [https://www.ebi.ac.uk/pdbsum/14gs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=14gs ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=14gs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=14gs OCA], [http://www.ebi.ac.uk/pdbsum/14gs PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=14gs RCSB]</span>
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== Function ==
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}}
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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/4g/14gs_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=14gs 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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Three-dimensional structures of the apo form of human pi class glutathione transferase have been determined by X-ray crystallography. The structures suggest the enzyme recognizes its substrate, glutathione, by an induced-fit mechanism. Compared to complexed forms of the enzyme, the environment around the catalytic residue, Tyr 7, remains unchanged in the apoenzyme. This observation supports the view that Tyr 7 does not act as a general base in the reaction mechanism. The observed cooperativity of the dimeric enzyme may be due to the movements of a helix that forms one wall of the active site and, in particular, to movements of a tyrosine residue that is located in the subunit interface.
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'''GLUTATHIONE S-TRANSFERASE P1-1 APO FORM 1'''
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Evidence for an induced-fit mechanism operating in pi class glutathione transferases.,Oakley AJ, Lo Bello M, Ricci G, Federici G, Parker MW Biochemistry. 1998 Jul 14;37(28):9912-7. PMID:9665696<ref>PMID:9665696</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 14gs" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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Three-dimensional structures of the apo form of human pi class glutathione transferase have been determined by X-ray crystallography. The structures suggest the enzyme recognizes its substrate, glutathione, by an induced-fit mechanism. Compared to complexed forms of the enzyme, the environment around the catalytic residue, Tyr 7, remains unchanged in the apoenzyme. This observation supports the view that Tyr 7 does not act as a general base in the reaction mechanism. The observed cooperativity of the dimeric enzyme may be due to the movements of a helix that forms one wall of the active site and, in particular, to movements of a tyrosine residue that is located in the subunit interface.
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*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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14GS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=14GS OCA].
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__TOC__
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</StructureSection>
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==Reference==
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Evidence for an induced-fit mechanism operating in pi class glutathione transferases., Oakley AJ, Lo Bello M, Ricci G, Federici G, Parker MW, Biochemistry. 1998 Jul 14;37(28):9912-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9665696 9665696]
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[[Category: Glutathione transferase]]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Bello, M Lo.]]
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[[Category: Federici G]]
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[[Category: Federici, G.]]
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[[Category: Lo Bello M]]
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[[Category: Oakley, A J.]]
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[[Category: Oakley AJ]]
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[[Category: Parker, M W.]]
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[[Category: Parker MW]]
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[[Category: Ricci, G.]]
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[[Category: Ricci G]]
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[[Category: apoenzyme]]
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[[Category: detoxification]]
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[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:28:14 2008''
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Current revision

GLUTATHIONE S-TRANSFERASE P1-1 APO FORM 1

PDB ID 14gs

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