View source for 6ezy


==ARABIDOPSIS THALIANA GSTF9, GSH AND GSOH BOUND==
<StructureSection load='6ezy' size='340' side='right' caption='[[6ezy]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6ezy]] 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=6EZY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EZY 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=GSH:GLUTATHIONE'>GSH</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5fqx|5fqx]], [[5fqy|5fqy]], [[5fqz|5fqz]], [[5fr4|5fr4]], [[5fr5|5fr5]]</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='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=6ezy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ezy OCA], [http://pdbe.org/6ezy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ezy RCSB], [http://www.ebi.ac.uk/pdbsum/6ezy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ezy 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>  
<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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6ezy" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Arath]]
[[Category: Glutathione transferase]]
[[Category: Messens, J]]
[[Category: Rosado, L]]
[[Category: Tossounian, M A]]
[[Category: VanMolle, I]]
[[Category: Vertommen, D]]
[[Category: Wahni, K]]
[[Category: Gsh]]
[[Category: Gsoh]]
[[Category: Peroxidase]]
[[Category: Phi class]]
[[Category: Transferase]]