7zs3
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7zs3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Populus_trichocarpa Populus trichocarpa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ZS3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ZS3 FirstGlance]. <br> | <table><tr><td colspan='2'>[[7zs3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Populus_trichocarpa Populus trichocarpa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ZS3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ZS3 FirstGlance]. <br> | ||
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></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]] 1.603Å</td></tr> |
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</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=7zs3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7zs3 OCA], [https://pdbe.org/7zs3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7zs3 RCSB], [https://www.ebi.ac.uk/pdbsum/7zs3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7zs3 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=7zs3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7zs3 OCA], [https://pdbe.org/7zs3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7zs3 RCSB], [https://www.ebi.ac.uk/pdbsum/7zs3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7zs3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
- | + | [https://www.uniprot.org/uniprot/B9HKX9_POPTR B9HKX9_POPTR] | |
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Glutathione transferases (GSTs) constitute a widespread superfamily of enzymes notably involved in xenobiotic detoxification and/or in specialized metabolism. Populus trichocarpa genome (V4.1 assembly, Phytozome 13) consists of 74 genes coding for full-length GSTs and ten likely pseudogenes. These GSTs are divided into 11 classes, in which the tau class (GSTU) is the most abundant with 54 isoforms. PtGSTU19 and 20, two paralogs sharing more than 91% sequence identity (95% of sequence similarity), would have diverged from a common ancestor of P. trichocarpa and P. yatungensis species. These enzymes display the distinctive glutathione (GSH)-conjugation and peroxidase activities against model substrates. The resolution of the crystal structures of these proteins revealed significant structural differences despite their high sequence identity. PtGSTU20 has a well-defined deep pocket in the active site whereas the bottom of this pocket is disordered in PtGSTU19. In a screen of potential ligands, we were able to identify an interaction with flavonoids. Some of them, previously identified in poplar (chrysin, galangin, and pinocembrin), inhibited GSH-conjugation activity of both enzymes with a more pronounced effect on PtGSTU20. The crystal structures of PtGSTU20 complexed with these molecules provide evidence for their potential involvement in flavonoid transport in P. trichocarpa. | ||
+ | |||
+ | Biochemical and Structural Insights on the Poplar Tau Glutathione Transferase GSTU19 and 20 Paralogs Binding Flavonoids.,Sylvestre-Gonon E, Morette L, Viloria M, Mathiot S, Boutilliat A, Favier F, Rouhier N, Didierjean C, Hecker A Front Mol Biosci. 2022 Aug 12;9:958586. doi: 10.3389/fmolb.2022.958586., eCollection 2022. PMID:36032685<ref>PMID:36032685</ref> | ||
+ | |||
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 7zs3" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> |
Current revision
Crystal structure of poplar glutathione transferase U19
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