3d5j
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3d5j]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D5J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3D5J FirstGlance]. <br> | <table><tr><td colspan='2'>[[3d5j]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D5J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3D5J FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3d4m|3d4m]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3d4m|3d4m]]</td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GRX2, TTR, TTR1, YDR513W, D9719.17 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GRX2, TTR, TTR1, YDR513W, D9719.17 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])</td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3d5j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d5j OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3d5j RCSB], [http://www.ebi.ac.uk/pdbsum/3d5j PDBsum]</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=3d5j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d5j OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3d5j RCSB], [http://www.ebi.ac.uk/pdbsum/3d5j PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/GLRX2_YEAST GLRX2_YEAST]] Multifunctional enzyme with glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S-transferase (GST) activity. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-protein-disulfides in a coupled system with glutathione reductase. Required for resistance to reactive oxygen species (ROS) by directly reducing hydroperoxides and for the detoxification of ROS-mediated damage.<ref>PMID:9571241</ref> <ref>PMID:11875065</ref> <ref>PMID:12684511</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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Structural aspects of the distinct biochemical properties of glutaredoxin 1 and glutaredoxin 2 from Saccharomyces cerevisiae.,Discola KF, de Oliveira MA, Rosa Cussiol JR, Monteiro G, Barcena JA, Porras P, Padilla CA, Guimaraes BG, Netto LE J Mol Biol. 2009 Jan 23;385(3):889-901. Epub 2008 Oct 28. PMID:18992757<ref>PMID:18992757</ref> | Structural aspects of the distinct biochemical properties of glutaredoxin 1 and glutaredoxin 2 from Saccharomyces cerevisiae.,Discola KF, de Oliveira MA, Rosa Cussiol JR, Monteiro G, Barcena JA, Porras P, Padilla CA, Guimaraes BG, Netto LE J Mol Biol. 2009 Jan 23;385(3):889-901. Epub 2008 Oct 28. PMID:18992757<ref>PMID:18992757</ref> | ||
| - | From | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
</div> | </div> | ||
== References == | == References == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
| - | [[Category: Barcena, J A | + | [[Category: Barcena, J A]] |
| - | [[Category: Discola, K F | + | [[Category: Discola, K F]] |
[[Category: Guimaraes, B G]] | [[Category: Guimaraes, B G]] | ||
| - | [[Category: Netto, L E.S | + | [[Category: Netto, L E.S]] |
| - | [[Category: Oliveira, M A.de | + | [[Category: Oliveira, M A.de]] |
| - | [[Category: Padilla, C A | + | [[Category: Padilla, C A]] |
| - | [[Category: Porras, P | + | [[Category: Porras, P]] |
[[Category: Electron transport]] | [[Category: Electron transport]] | ||
[[Category: Mitochondrion]] | [[Category: Mitochondrion]] | ||
Revision as of 00:33, 25 December 2014
Structure of yeast Grx2-C30S mutant with glutathionyl mixed disulfide
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