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| | ==The structure of DHAR1 from Arabidopsis thaliana== | | ==The structure of DHAR1 from Arabidopsis thaliana== |
| - | <StructureSection load='5elg' size='340' side='right' caption='[[5elg]], [[Resolution|resolution]] 1.81Å' scene=''> | + | <StructureSection load='5elg' size='340' side='right'caption='[[5elg]], [[Resolution|resolution]] 1.81Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5elg]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ELG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ELG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5elg]] is a 1 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=5ELG OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5ELG FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene></td></tr> |
| | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DHAR1, DHAR5, At1g19570, F14P1.9, F18O14.22 ([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='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=5elg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5elg OCA], [http://pdbe.org/5elg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5elg RCSB], [http://www.ebi.ac.uk/pdbsum/5elg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5elg ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5elg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5elg OCA], [http://pdbe.org/5elg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5elg RCSB], [http://www.ebi.ac.uk/pdbsum/5elg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5elg ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5elg" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5elg" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Arath]] |
| | [[Category: Glutathione transferase]] | | [[Category: Glutathione transferase]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Lapthorn, A J]] | | [[Category: Lapthorn, A J]] |
| | [[Category: Menault, M]] | | [[Category: Menault, M]] |
| Structural highlights
5elg is a 1 chain structure with sequence from Arath. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , |
| Gene: | DHAR1, DHAR5, At1g19570, F14P1.9, F18O14.22 (ARATH) |
| Activity: | Glutathione transferase, with EC number 2.5.1.18 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[DHAR1_ARATH] Displays a dual function. As a soluble protein, exhibits glutathione-dependent thiol transferase and dehydroascorbate (DHA) reductase activities. Key component of the ascorbate recycling system. Involved in the redox homeostasis, especially in scavenging of ROS under oxidative stresses, subsequently to biotic or abiotic inducers. As a peripheral membrane protein, could also function as voltage-gated ion channel.[1] [2] [3]
Publication Abstract from PubMed
Searches with the human Omega glutathione transferase (GST) identified two outlying groups of the GST superfamily in Arabidopsis thaliana which differed from all other plant GSTs by containing a cysteine in place of a serine at the active site. One group consisted of four genes, three of which encoded active glutathione-dependent dehydroascorbate reductases (DHARs). Two DHARs were predicted to be cytosolic, whereas the other contained a chloroplast targeting peptide. The DHARs were also active as thiol transferases but had no glutathione conjugating activity. Unlike most other GSTs, DHARs were monomeric. The other class of GST comprised two genes termed the Lambda GSTs (GSTLs). The recombinant GSTLs were also monomeric and had glutathione-dependent thiol transferase activity. One GSTL was cytosolic, whereas the other was chloroplast-targeted. When incubated with oxidized glutathione, the putative active site cysteine of the GSTLs and cytosolic DHARs formed mixed disulfides with glutathione, whereas the plastidic DHAR formed an intramolecular disulfide. DHAR S-glutathionylation was consistent with a proposed catalytic mechanism for dehydroascorbate reduction. Roles for the cytosolic DHARs and GSTLs as antioxidant enzymes were also inferred from the induction of the respective genes following exposure to chemicals and oxidative stress.
Functional divergence in the glutathione transferase superfamily in plants. Identification of two classes with putative functions in redox homeostasis in Arabidopsis thaliana.,Dixon DP, Davis BG, Edwards R J Biol Chem. 2002 Aug 23;277(34):30859-69. Epub 2002 Jun 19. PMID:12077129[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Dixon DP, Davis BG, Edwards R. Functional divergence in the glutathione transferase superfamily in plants. Identification of two classes with putative functions in redox homeostasis in Arabidopsis thaliana. J Biol Chem. 2002 Aug 23;277(34):30859-69. Epub 2002 Jun 19. PMID:12077129 doi:http://dx.doi.org/10.1074/jbc.M202919200
- ↑ Sasaki-Sekimoto Y, Taki N, Obayashi T, Aono M, Matsumoto F, Sakurai N, Suzuki H, Hirai MY, Noji M, Saito K, Masuda T, Takamiya K, Shibata D, Ohta H. Coordinated activation of metabolic pathways for antioxidants and defence compounds by jasmonates and their roles in stress tolerance in Arabidopsis. Plant J. 2005 Nov;44(4):653-68. PMID:16262714 doi:http://dx.doi.org/10.1111/j.1365-313X.2005.02560.x
- ↑ Elter A, Hartel A, Sieben C, Hertel B, Fischer-Schliebs E, Luttge U, Moroni A, Thiel G. A plant homolog of animal chloride intracellular channels (CLICs) generates an ion conductance in heterologous systems. J Biol Chem. 2007 Mar 23;282(12):8786-92. Epub 2007 Jan 31. PMID:17267397 doi:http://dx.doi.org/10.1074/jbc.M607241200
- ↑ Dixon DP, Davis BG, Edwards R. Functional divergence in the glutathione transferase superfamily in plants. Identification of two classes with putative functions in redox homeostasis in Arabidopsis thaliana. J Biol Chem. 2002 Aug 23;277(34):30859-69. Epub 2002 Jun 19. PMID:12077129 doi:http://dx.doi.org/10.1074/jbc.M202919200
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