4ags
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 4ags is ON HOLD until Paper Publication Authors: Fyfe, P.K., Westrop, G.D., Silva, A.M., Coombs, G.H., Hunter, W.N. Description: Leishmania TDR1 -a...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Leishmania TDR1 - a unique trimeric glutathione transferase== | |
| + | <StructureSection load='4ags' size='340' side='right'caption='[[4ags]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4ags]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Leishmania_infantum Leishmania infantum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AGS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AGS 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]] 2.3Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=4ags FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ags OCA], [https://pdbe.org/4ags PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ags RCSB], [https://www.ebi.ac.uk/pdbsum/4ags PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ags ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A4I8P2_LEIIN A4I8P2_LEIIN] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Thiol-dependent reductase I (TDR1), an enzyme found in parasitic Leishmania species and Trypanosoma cruzi, is implicated in deglutathionylation and activation of antimonial prodrugs used to treat leishmaniasis. The 2.3 A resolution structure of TDR1 reveals a unique trimer of subunits each containing two glutathione-S-transferase (GST) domains. The similarities of individual domains and comparisons with GST classes suggest that TDR1 evolved by gene duplication, diversification, and gene fusion; a combination of events previously unknown in the GST protein superfamily and potentially explaining the distinctive enzyme properties of TDR1. The deglutathionylation activity of TDR1 implies that glutathione itself has regulatory intracellular roles in addition to being a precursor for trypanothione, the major low mass thiol present in trypanosomatids. We propose that activation of antiparasite Sb(V)-drugs is a legacy of the deglutathionylation activity of TDR1 and involves processing glutathione adducts with concomitant reduction of the metalloid to active Sb(III) species. | ||
| - | + | Leishmania TDR1 structure, a unique trimeric glutathione transferase capable of deglutathionylation and antimonial prodrug activation.,Fyfe PK, Westrop GD, Silva AM, Coombs GH, Hunter WN Proc Natl Acad Sci U S A. 2012 Jul 2. PMID:22753509<ref>PMID:22753509</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4ags" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Leishmania infantum]] | ||
| + | [[Category: Coombs GH]] | ||
| + | [[Category: Fyfe PK]] | ||
| + | [[Category: Hunter WN]] | ||
| + | [[Category: Silva AM]] | ||
| + | [[Category: Westrop GD]] | ||
Current revision
Leishmania TDR1 - a unique trimeric glutathione transferase
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