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16gs
From Proteopedia
(Difference between revisions)
(New page: 200px<br /> <applet load="16gs" size="450" color="white" frame="true" align="right" spinBox="true" caption="16gs, resolution 1.90Å" /> '''GLUTATHIONE S-TRANS...) |
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| - | [[Image:16gs.gif|left|200px]]<br /> | ||
| - | <applet load="16gs" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="16gs, resolution 1.90Å" /> | ||
| - | '''GLUTATHIONE S-TRANSFERASE P1-1 APO FORM 3'''<br /> | ||
| - | == | + | ==GLUTATHIONE S-TRANSFERASE P1-1 APO FORM 3== |
| - | Three-dimensional structures of the apo form of human pi class glutathione | + | <StructureSection load='16gs' size='340' side='right'caption='[[16gs]], [[Resolution|resolution]] 1.90Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[16gs]] 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=16GS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=16GS FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | ||
| + | <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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=16gs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=16gs OCA], [https://pdbe.org/16gs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=16gs RCSB], [https://www.ebi.ac.uk/pdbsum/16gs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=16gs ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [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> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/6g/16gs_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=16gs ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 16gs" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Federici G]] | ||
| + | [[Category: Lo Bello M]] | ||
| + | [[Category: Oakley AJ]] | ||
| + | [[Category: Parker MW]] | ||
| + | [[Category: Ricci G]] | ||
Current revision
GLUTATHIONE S-TRANSFERASE P1-1 APO FORM 3
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