|
|
| Line 1: |
Line 1: |
| | | | |
| | ==ARABIDOPSIS THALIANA GSTF9, GSO3 AND GSOH BOUND== | | ==ARABIDOPSIS THALIANA GSTF9, GSO3 AND GSOH BOUND== |
| - | <StructureSection load='6f01' size='340' side='right' caption='[[6f01]], [[Resolution|resolution]] 2.50Å' scene=''> | + | <StructureSection load='6f01' size='340' side='right'caption='[[6f01]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == 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]] 2.5Å</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> | | </table> |
| | == Function == | | == 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®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 6f01" style="background-color:#fffaf0;"></div>
| + | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </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]]
| + | |
