14gs: Difference between revisions
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<StructureSection load='14gs' size='340' side='right'caption='[[14gs]], [[Resolution|resolution]] 2.80Å' scene=''> | <StructureSection load='14gs' size='340' side='right'caption='[[14gs]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[14gs]] is a 2 chain structure. 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> | <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> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</td></tr> | ||
<tr id=' | <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> | ||
<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> | <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> | ||
</table> | </table> | ||
== Function == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Federici G]] | ||
[[Category: | [[Category: Lo Bello M]] | ||
[[Category: Oakley | [[Category: Oakley AJ]] | ||
[[Category: Parker | [[Category: Parker MW]] | ||
[[Category: Ricci | [[Category: Ricci G]] | ||
Latest revision as of 13:42, 2 August 2023
GLUTATHIONE S-TRANSFERASE P1-1 APO FORM 1GLUTATHIONE S-TRANSFERASE P1-1 APO FORM 1
Structural highlights
FunctionGSTP1_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.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThree-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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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