6f01: Difference between revisions

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 ==ARABIDOPSIS THALIANA GSTF9, GSO3 AND GSOH BOUND==
-<StructureSection load='6f01' size='340' side='right' caption='[[6f01]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
+<StructureSection load='6f01' size='340' side='right'caption='[[6f01]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6f01]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6F01 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6F01 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6f01]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6F01 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6F01 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=GS8:S-HYDROXY-GLUTATHIONE'>GS8</scene>, <scene name='pdbligand=GTS:GLUTATHIONE+SULFONIC+ACID'>GTS</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]] 2.5&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6ezy|6ezy]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=GS8:S-HYDROXY-GLUTATHIONE'>GS8</scene>, <scene name='pdbligand=GTS:GLUTATHIONE+SULFONIC+ACID'>GTS</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GSTF9, GLUTTR, GSTF7, At2g30860, F7F1.7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</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=6f01 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f01 OCA], [https://pdbe.org/6f01 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6f01 RCSB], [https://www.ebi.ac.uk/pdbsum/6f01 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6f01 ProSAT]</span></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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6f01 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f01 OCA], [http://pdbe.org/6f01 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6f01 RCSB], [http://www.ebi.ac.uk/pdbsum/6f01 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6f01 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/GSTF9_ARATH GSTF9_ARATH]] In vitro, possesses glutathione S-transferase activity toward 1-chloro-2,4-dinitrobenzene (CDNB) and benzyl isothiocyanate (BITC), and glutathione peroxidase activity toward cumene hydroperoxide and linoleic acid-13-hydroperoxide. May be involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles and have a detoxification role against certain herbicides.<ref>PMID:12090627</ref> <ref>PMID:16538523</ref>
+[https://www.uniprot.org/uniprot/GSTF9_ARATH GSTF9_ARATH] In vitro, possesses glutathione S-transferase activity toward 1-chloro-2,4-dinitrobenzene (CDNB) and benzyl isothiocyanate (BITC), and glutathione peroxidase activity toward cumene hydroperoxide and linoleic acid-13-hydroperoxide. May be involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles and have a detoxification role against certain herbicides.<ref>PMID:12090627</ref> <ref>PMID:16538523</ref>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Glutathione transferase enzymes help plants to cope with biotic and abiotic stress. They mainly catalyze the conjugation of glutathione (GSH) onto xenobiotics, and some act as glutathione peroxidase. With X-ray crystallography, kinetics, and thermodynamics, we studied the impact of oxidation on Arabidopsis thaliana glutathione transferase Phi 9 (GSTF9). GSTF9 has no cysteine in its sequence, and it adopts a universal GST structural fold characterized by a typical conserved GSH-binding site (G-site) and a hydrophobic co-substrate-binding site (H-site). At elevated H2 O2 concentrations, methionine sulfur oxidation decreases its transferase activity. This oxidation increases the flexibility of the H-site loop, which is reflected in lower activities for hydrophobic substrates. Determination of the transition state thermodynamic parameters shows that upon oxidation an increased enthalpic penalty is counterbalanced by a more favorable entropic contribution. All in all, to guarantee functionality under oxidative stress conditions, GSTF9 employs a thermodynamic and structural compensatory mechanism and becomes substrate of methionine sulfoxide reductases, making it a redox-regulated enzyme.
-Redox-regulated methionine oxidation of Arabidopsis thaliana glutathione transferase Phi9 induces H-site flexibility.,Tossounian MA, Wahni K, Van Molle I, Vertommen D, Astolfi Rosado L, Messens J Protein Sci. 2018 May 7. doi: 10.1002/pro.3440. PMID:29732642<ref>PMID:29732642</ref>
+==See Also==
+*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 6f01" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Arath]]
+[[Category: Arabidopsis thaliana]]
-[[Category: Glutathione transferase]]
+[[Category: Large Structures]]
-[[Category: Messens, J]]
+[[Category: Messens J]]
-[[Category: Molle, I Van]]
+[[Category: Rosado L]]
-[[Category: Rosado, L]]
+[[Category: Tossounian MA]]
-[[Category: Tossounian, M A]]
+[[Category: Van Molle I]]
-[[Category: Vertommen, D]]
+[[Category: Vertommen D]]
-[[Category: Wahni, K]]
+[[Category: Wahni K]]
-[[Category: Gso3]]
-[[Category: Gsoh]]
-[[Category: Peroxidase]]
-[[Category: Phi class]]
-[[Category: Transferase]]