|
|
| Line 3: |
Line 3: |
| <StructureSection load='3rpp' size='340' side='right'caption='[[3rpp]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='3rpp' size='340' side='right'caption='[[3rpp]], [[Resolution|resolution]] 1.80Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[3rpp]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RPP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RPP FirstGlance]. <br> | | <table><tr><td colspan='2'>[[3rpp]] is a 3 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=3RPP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RPP FirstGlance]. <br> |
| </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3rpn|3rpn]]</div></td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GSTK1, HDCMD47P ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
| |
| <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] </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=3rpp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rpp OCA], [https://pdbe.org/3rpp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rpp RCSB], [https://www.ebi.ac.uk/pdbsum/3rpp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rpp 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=3rpp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rpp OCA], [https://pdbe.org/3rpp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rpp RCSB], [https://www.ebi.ac.uk/pdbsum/3rpp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rpp ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
| [[https://www.uniprot.org/uniprot/GSTK1_HUMAN GSTK1_HUMAN]] Significant glutathione conjugating activity is found only with the model substrate, 1-chloro-2,4-dinitrobenzene (CDNB).
| | [https://www.uniprot.org/uniprot/GSTK1_HUMAN GSTK1_HUMAN] Significant glutathione conjugating activity is found only with the model substrate, 1-chloro-2,4-dinitrobenzene (CDNB). |
| <div style="background-color:#fffaf0;">
| |
| == Publication Abstract from PubMed ==
| |
| GSTs (glutathione transferases) are a family of enzymes that primarily catalyse nucleophilic addition of the thiol of GSH (reduced glutathione) to a variety of hydrophobic electrophiles in the cellular detoxification of cytotoxic and genotoxic compounds. GSTks (Kappa class GSTs) are a distinct class because of their unique cellular localization, function and structure. In the present paper we report the crystal structures of hGSTk (human GSTk) in apo-form and in complex with GTX (S-hexylglutathione) and steady-state kinetic studies, revealing insights into the catalytic mechanism of hGSTk and other GSTks. Substrate binding induces a conformational change of the active site from an 'open' conformation in the apo-form to a 'closed' conformation in the GTX-bound complex, facilitating formations of the G site (GSH-binding site) and the H site (hydrophobic substrate-binding site). The conserved Ser(16) at the G site functions as the catalytic residue in the deprotonation of the thiol group and the conserved Asp(69), Ser(200), Asp(201) and Arg(202) form a network of interactions with gamma-glutamyl carboxylate to stabilize the thiolate anion. The H site is a large hydrophobic pocket with conformational flexibility to allow the binding of different hydrophobic substrates. The kinetic mechanism of hGSTk conforms to a rapid equilibrium random sequential Bi Bi model.
| |
| | |
| Crystal structures and kinetic studies of human Kappa class glutathione transferase provide insights into the catalytic mechanism.,Wang B, Peng Y, Zhang T, Ding J Biochem J. 2011 Oct 15;439(2):215-25. PMID:21728995<ref>PMID:21728995</ref>
| |
| | |
| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| |
| </div>
| |
| <div class="pdbe-citations 3rpp" style="background-color:#fffaf0;"></div>
| |
|
| |
|
| ==See Also== | | ==See Also== |
| *[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]] | | *[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]] |
| == References ==
| |
| <references/>
| |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Glutathione transferase]] | | [[Category: Homo sapiens]] |
| [[Category: Human]]
| |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Ding, J]] | | [[Category: Ding J]] |
| [[Category: Peng, Y]] | | [[Category: Peng Y]] |
| [[Category: Wang, B]] | | [[Category: Wang B]] |
| [[Category: Zhang, T]] | | [[Category: Zhang T]] |
| [[Category: Apo form]]
| |
| [[Category: Detoxification]]
| |
| [[Category: Gsh binding]]
| |
| [[Category: Kappa gst]]
| |
| [[Category: Transferase]]
| |
| [[Category: Trx domain]]
| |
