6gcc: Difference between revisions
New page: '''Unreleased structure''' The entry 6gcc is ON HOLD until Paper Publication Authors: Schwartz, M., Favier, F., Didierjean, C. Description: Crystal structure of glutathione transferase... |
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==Crystal structure of glutathione transferase Xi 3 mutant C56S from Trametes versicolor in complex with dextran-sulfate== | |||
<StructureSection load='6gcc' size='340' side='right' caption='[[6gcc]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6gcc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bjerkandera_versicolor Bjerkandera versicolor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GCC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GCC FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EU8:[(2~{R},3~{R},4~{R},5~{R},6~{R})-2-[[(2~{S},3~{S},4~{S},5~{R},6~{R})-6-[[(2~{S},3~{R},4~{R},5~{R},6~{R})-6-(hydroxymethyl)-3-oxidanyl-4,5-disulfooxy-oxan-2-yl]oxymethyl]-3-oxidanyl-4,5-disulfooxy-oxan-2-yl]oxymethyl]-3,5,6-trisulfooxy-oxan-4-yl]+hydrogen+sulfate'>EU8</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6gcc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gcc OCA], [http://pdbe.org/6gcc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gcc RCSB], [http://www.ebi.ac.uk/pdbsum/6gcc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gcc ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Glutathione transferases (GSTs) from the Xi and Omega classes have a catalytic cysteine residue, which gives them reductase activities. Until now, they have been assigned distinct substrates. While Xi GSTs specifically reduce glutathionyl-(hydro)quinones, Omega GSTs are specialized in the reduction of glutathionyl-acetophenones. Here, we present the biochemical and structural analysis of TvGSTX1 and TvGSTX3 isoforms from the wood-degrading fungus Trametes versicolor. TvGSTX1 reduces GS-menadione as expected, while TvGSTX3 reduces both Xi and Omega substrates. An in-depth structural analysis indicates a broader active site for TvGSTX3 due to specific differences in the nature of the residues situated in the C-terminal helix alpha9. This feature could explain the catalytic duality of TvGSTX3. Based on phylogenetic analysis, we propose that this duality might exist in saprophytic fungi and ascomycetes. This article is protected by copyright. All rights reserved. | |||
Trametes versicolor Glutathione Transferase Xi 3, a dual Cys-GST with catalytic specificities of both Xi and Omega classes.,Schwartz M, Perrot T, Deroy A, Roret T, Morel-Rouhier M, Mulliert G, Gelhaye E, Favier F, Didierjean C FEBS Lett. 2018 Aug 15. doi: 10.1002/1873-3468.13224. PMID:30112765<ref>PMID:30112765</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[Category: | <div class="pdbe-citations 6gcc" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bjerkandera versicolor]] | |||
[[Category: Didierjean, C]] | [[Category: Didierjean, C]] | ||
[[Category: Favier, F]] | [[Category: Favier, F]] | ||
[[Category: Schwartz, M]] | |||
[[Category: Glutathione transferase]] | |||
[[Category: Transferase]] | |||
Latest revision as of 11:53, 3 October 2018
Crystal structure of glutathione transferase Xi 3 mutant C56S from Trametes versicolor in complex with dextran-sulfateCrystal structure of glutathione transferase Xi 3 mutant C56S from Trametes versicolor in complex with dextran-sulfate
Structural highlights
Publication Abstract from PubMedGlutathione transferases (GSTs) from the Xi and Omega classes have a catalytic cysteine residue, which gives them reductase activities. Until now, they have been assigned distinct substrates. While Xi GSTs specifically reduce glutathionyl-(hydro)quinones, Omega GSTs are specialized in the reduction of glutathionyl-acetophenones. Here, we present the biochemical and structural analysis of TvGSTX1 and TvGSTX3 isoforms from the wood-degrading fungus Trametes versicolor. TvGSTX1 reduces GS-menadione as expected, while TvGSTX3 reduces both Xi and Omega substrates. An in-depth structural analysis indicates a broader active site for TvGSTX3 due to specific differences in the nature of the residues situated in the C-terminal helix alpha9. This feature could explain the catalytic duality of TvGSTX3. Based on phylogenetic analysis, we propose that this duality might exist in saprophytic fungi and ascomycetes. This article is protected by copyright. All rights reserved. Trametes versicolor Glutathione Transferase Xi 3, a dual Cys-GST with catalytic specificities of both Xi and Omega classes.,Schwartz M, Perrot T, Deroy A, Roret T, Morel-Rouhier M, Mulliert G, Gelhaye E, Favier F, Didierjean C FEBS Lett. 2018 Aug 15. doi: 10.1002/1873-3468.13224. PMID:30112765[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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