1gss: Difference between revisions

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-[[Image:1gss.gif|left|200px]]<br />
-<applet load="1gss" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1gss, resolution 2.8&Aring;" />
-'''THREE-DIMENSIONAL STRUCTURE OF CLASS PI GLUTATHIONE S-TRANSFERASE FROM HUMAN PLACENTA IN COMPLEX WITH S-HEXYLGLUTATHIONE AT 2.8 ANGSTROMS RESOLUTION'''<br />
-==Overview==
+==THREE-DIMENSIONAL STRUCTURE OF CLASS PI GLUTATHIONE S-TRANSFERASE FROM HUMAN PLACENTA IN COMPLEX WITH S-HEXYLGLUTATHIONE AT 2.8 ANGSTROMS RESOLUTION==
-The three-dimensional structure of human class pi glutathione, S-transferase from placenta (hGSTP1-1), a homodimeric enzyme, has been, solved by Patterson search methods and refined at 2.8 A resolution to a, final crystallographic R-factor of 19.6% (8.0 to 2.8 A resolution)., Subunit folding topology, subunit overall structure and subunit, association closely resembles the structure of porcine class pi, glutathione S-transferase. The binding site of a competitive inhibitor, S-hexylglutathione, is analyzed and the locations of the binding regions, for glutathione (G-site) and electrophilic substrates (H-site) are, determined. The specific interactions between protein and the inhibitor's, glutathione peptide are the same as those observed between glutathione, sulfonate and the porcine isozyme. The H-site is located adjacent to the, G-site, with the hexyl moiety lying above a segment (residues 8 to 10), connecting strand beta 1 and helix alpha A where it is in hydrophobic, contact with Tyr7, Phe8, Val10, Val35 and Tyr106. Catalytic models are, discussed on the basis of the molecular structure.
+<StructureSection load='1gss' size='340' side='right'caption='[[1gss]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1gss]] 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=1GSS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GSS 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]] 2.8&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LEE:L-GAMMA-GLUTAMYL-S-HEXYL-L-CYSTEINYLGLYCINE'>LEE</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=1gss FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gss OCA], [https://pdbe.org/1gss PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gss RCSB], [https://www.ebi.ac.uk/pdbsum/1gss PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gss 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/gs/1gss_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=1gss ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-GSS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. 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=1GSS OCA].
+*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
+== References ==
-==Reference==
+<references/>
-Three-dimensional structure of class pi glutathione S-transferase from human placenta in complex with S-hexylglutathione at 2.8 A resolution., Reinemer P, Dirr HW, Ladenstein R, Huber R, Lo Bello M, Federici G, Parker MW, J Mol Biol. 1992 Sep 5;227(1):214-26. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1522586 1522586]
+__TOC__
-[[Category: Glutathione transferase]]
+</StructureSection>
-[[Category: Single protein]]
+[[Category: Homo sapiens]]
-[[Category: Dirr, H.W.]]
+[[Category: Large Structures]]
-[[Category: Federici, G.]]
+[[Category: Dirr HW]]
-[[Category: Huber, R.]]
+[[Category: Federici G]]
-[[Category: Ladenstein, R.]]
+[[Category: Huber R]]
-[[Category: Lobello, M.]]
+[[Category: Ladenstein R]]
-[[Category: Parker, M.W.]]
+[[Category: Lobello M]]
-[[Category: Reinemer, P.]]
+[[Category: Parker MW]]
-[[Category: transferase(glutathione)]]
+[[Category: Reinemer P]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:08:50 2007''