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| | <StructureSection load='4lmw' size='340' side='right'caption='[[4lmw]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='4lmw' size='340' side='right'caption='[[4lmw]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4lmw]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chrysosporium_pruinosum_(gilman_&_abbott)_carmich. Chrysosporium pruinosum (gilman & abbott) carmich.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LMW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LMW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4lmw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Phanerodontia_chrysosporium Phanerodontia chrysosporium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LMW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LMW FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</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]] 2.099Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4f03|4f03]], [[4g19|4g19]], [[4lmv|4lmv]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://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=4lmw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lmw OCA], [https://pdbe.org/4lmw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lmw RCSB], [https://www.ebi.ac.uk/pdbsum/4lmw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lmw ProSAT]</span></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=4lmw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lmw OCA], [http://pdbe.org/4lmw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4lmw RCSB], [http://www.ebi.ac.uk/pdbsum/4lmw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4lmw ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A067XG73_PHACH A0A067XG73_PHACH] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Glutathione transferase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Didierjean, C]] | + | [[Category: Phanerodontia chrysosporium]] |
| - | [[Category: Favier, F]] | + | [[Category: Didierjean C]] |
| - | [[Category: Prosper, P]] | + | [[Category: Favier F]] |
| - | [[Category: Gst fold]] | + | [[Category: Prosper P]] |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
A0A067XG73_PHACH
Publication Abstract from PubMed
Glutathione transferases (GSTs) form a superfamily of multifunctional proteins with essential roles in cellular detoxification processes and endogenous metabolism. The distribution of fungal-specific class A GSTs was investigated in saprotrophic fungi revealing a recent diversification within this class. Biochemical characterization of eight GSTFuA isoforms from Phanerochaete chrysosporium and Coprinus cinereus demonstrated functional diversity in saprotrophic fungi. The three-dimensional structures of three P. chrysosporium isoforms feature structural differences explaining the functional diversity of these enzymes. Competition experiments between fluorescent probes, and various molecules, showed that these GSTs function as ligandins with various small aromatic compounds, derived from lignin degradation or not, at a L-site overlapping the glutathione binding pocket. By combining genomic data with structural and biochemical determinations, we propose that this class of GST has evolved in response to environmental constraints induced by wood chemistry.
Diversification of fungal specific class a glutathione transferases in saprotrophic fungi.,Mathieu Y, Prosper P, Favier F, Harvengt L, Didierjean C, Jacquot JP, Morel-Rouhier M, Gelhaye E PLoS One. 2013 Nov 20;8(11):e80298. doi: 10.1371/journal.pone.0080298., eCollection 2013. PMID:24278272[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Mathieu Y, Prosper P, Favier F, Harvengt L, Didierjean C, Jacquot JP, Morel-Rouhier M, Gelhaye E. Diversification of fungal specific class a glutathione transferases in saprotrophic fungi. PLoS One. 2013 Nov 20;8(11):e80298. doi: 10.1371/journal.pone.0080298., eCollection 2013. PMID:24278272 doi:http://dx.doi.org/10.1371/journal.pone.0080298
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