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| | <StructureSection load='2gwd' size='340' side='right'caption='[[2gwd]], [[Resolution|resolution]] 2.09Å' scene=''> | | <StructureSection load='2gwd' size='340' side='right'caption='[[2gwd]], [[Resolution|resolution]] 2.09Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2gwd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Braju Braju]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GWD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GWD FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2gwd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Brassica_juncea Brassica juncea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GWD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GWD FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.09Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2gwc|2gwc]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GSH1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3707 BRAJU])</td></tr> | + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glutamate--cysteine_ligase Glutamate--cysteine ligase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.2 6.3.2.2] </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=2gwd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gwd OCA], [https://pdbe.org/2gwd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gwd RCSB], [https://www.ebi.ac.uk/pdbsum/2gwd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gwd ProSAT]</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=2gwd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gwd OCA], [https://pdbe.org/2gwd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gwd RCSB], [https://www.ebi.ac.uk/pdbsum/2gwd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gwd ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/GSH1_BRAJU GSH1_BRAJU]] Participates in the detoxification process.<ref>PMID:9620267</ref> <ref>PMID:9119067</ref>
| + | [https://www.uniprot.org/uniprot/GSH1_BRAJU GSH1_BRAJU] Participates in the detoxification process.<ref>PMID:9620267</ref> <ref>PMID:9119067</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Braju]] | + | [[Category: Brassica juncea]] |
| - | [[Category: Glutamate--cysteine ligase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Gromes, R]] | + | [[Category: Gromes R]] |
| - | [[Category: Hothorn, M]] | + | [[Category: Hothorn M]] |
| - | [[Category: Rausch, T]] | + | [[Category: Rausch T]] |
| - | [[Category: Scheffzek, K]] | + | [[Category: Scheffzek K]] |
| - | [[Category: Stuwe, T]] | + | [[Category: Stuwe T]] |
| - | [[Category: Wachter, A]] | + | [[Category: Wachter A]] |
| - | [[Category: Beta-hairpin]]
| + | |
| - | [[Category: Disulfide bridge]]
| + | |
| - | [[Category: Glutathione biosynthesis]]
| + | |
| - | [[Category: Ligase]]
| + | |
| - | [[Category: Redox regulation]]
| + | |
| Structural highlights
Function
GSH1_BRAJU Participates in the detoxification process.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Glutathione (GSH) plays a crucial role in plant metabolism and stress response. The rate-limiting step in the biosynthesis of GSH is catalyzed by glutamate cysteine ligase (GCL) the activity of which is tightly regulated. The regulation of plant GCLs is poorly understood. The crystal structure of substrate-bound GCL from Brassica juncea at 2.1-A resolution reveals a plant-unique regulatory mechanism based on two intramolecular redox-sensitive disulfide bonds. Reduction of one disulfide bond allows a beta-hairpin motif to shield the active site of B. juncea GCL, thereby preventing the access of substrates. Reduction of the second disulfide bond reversibly controls dimer to monomer transition of B. juncea GCL that is associated with a significant inactivation of the enzyme. These regulatory events provide a molecular link between high GSH levels in the plant cell and associated down-regulation of its biosynthesis. Furthermore, known mutations in the Arabidopsis GCL gene affect residues in the close proximity of the active site and thus explain the decreased GSH levels in mutant plants. In particular, the mutation in rax1-1 plants causes impaired binding of cysteine.
Structural basis for the redox control of plant glutamate cysteine ligase.,Hothorn M, Wachter A, Gromes R, Stuwe T, Rausch T, Scheffzek K J Biol Chem. 2006 Sep 15;281(37):27557-65. Epub 2006 Jun 9. PMID:16766527[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Schafer HJ, Haag-Kerwer A, Rausch T. cDNA cloning and expression analysis of genes encoding GSH synthesis in roots of the heavy-metal accumulator Brassica juncea L.: evidence for Cd-induction of a putative mitochondrial gamma-glutamylcysteine synthetase isoform. Plant Mol Biol. 1998 May;37(1):87-97. PMID:9620267
- ↑ Schafer HJ, Greiner S, Rausch T, Haag-Kerwer A. In seedlings of the heavy metal accumulator Brassica juncea Cu2+ differentially affects transcript amounts for gamma-glutamylcysteine synthetase (gamma-ECS) and metallothionein (MT2). FEBS Lett. 1997 Mar 10;404(2-3):216-20. PMID:9119067
- ↑ Hothorn M, Wachter A, Gromes R, Stuwe T, Rausch T, Scheffzek K. Structural basis for the redox control of plant glutamate cysteine ligase. J Biol Chem. 2006 Sep 15;281(37):27557-65. Epub 2006 Jun 9. PMID:16766527 doi:10.1074/jbc.M602770200
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