8a0q: Difference between revisions
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==Crystal structure of poplar glutathione transferase U20 in complex with baicalein== | ==Crystal structure of poplar glutathione transferase U20 in complex with baicalein== | ||
<StructureSection load='8a0q' size='340' side='right'caption='[[8a0q]]' scene=''> | <StructureSection load='8a0q' size='340' side='right'caption='[[8a0q]], [[Resolution|resolution]] 2.05Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8A0Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8A0Q FirstGlance]. <br> | <table><tr><td colspan='2'>[[8a0q]] 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=8A0Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8A0Q FirstGlance]. <br> | ||
</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=8a0q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8a0q OCA], [https://pdbe.org/8a0q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8a0q RCSB], [https://www.ebi.ac.uk/pdbsum/8a0q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8a0q ProSAT]</span></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]] 2.048Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3WL:5,6,7-TRIHYDROXY-2-PHENYL-4H-CHROMEN-4-ONE'>3WL</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=8a0q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8a0q OCA], [https://pdbe.org/8a0q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8a0q RCSB], [https://www.ebi.ac.uk/pdbsum/8a0q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8a0q ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/D2X9R3_POPTR D2X9R3_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 8a0q" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Populus trichocarpa]] | |||
[[Category: Didierjean C]] | [[Category: Didierjean C]] | ||
[[Category: Favier F]] | [[Category: Favier F]] | ||
Latest revision as of 16:36, 1 February 2024
Crystal structure of poplar glutathione transferase U20 in complex with baicaleinCrystal structure of poplar glutathione transferase U20 in complex with baicalein
Structural highlights
FunctionPublication Abstract from PubMedGlutathione 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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