4lmw

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Current revision

Crystal structure of glutathione transferase GSTFuA3 from Phanerochaete chrysosporium

Structural highlights

4lmw is a 1 chain structure with sequence from Phanerodontia chrysosporium. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.099Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

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OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4lmw"

@@ Line 1: / Line 1: @@
 ==Crystal structure of glutathione transferase GSTFuA3 from Phanerochaete chrysosporium==
-<StructureSection load='4lmw' size='340' side='right' caption='[[4lmw]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
+<StructureSection load='4lmw' size='340' side='right'caption='[[4lmw]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4lmw]] is a 1 chain structure. 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]] 2.099&#8491;</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>
+== Function ==
+[https://www.uniprot.org/uniprot/A0A067XG73_PHACH A0A067XG73_PHACH]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Glutathione transferase]]
+[[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]]

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