3d5j
From Proteopedia
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==Structure of yeast Grx2-C30S mutant with glutathionyl mixed disulfide== | ==Structure of yeast Grx2-C30S mutant with glutathionyl mixed disulfide== | ||
| - | <StructureSection load='3d5j' size='340' side='right' caption='[[3d5j]], [[Resolution|resolution]] 1.91Å' scene=''> | + | <StructureSection load='3d5j' size='340' side='right'caption='[[3d5j]], [[Resolution|resolution]] 1.91Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3d5j]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3d5j]] is a 2 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=3D5J FirstGlance]. <br> |
| - | </td></tr><tr><td class="sblockLbl"><b>[[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.91Å</td></tr> |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene></td></tr> | |
| - | <tr><td class="sblockLbl"><b>[[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3d5j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d5j OCA], [https://pdbe.org/3d5j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3d5j RCSB], [https://www.ebi.ac.uk/pdbsum/3d5j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3d5j ProSAT]</span></td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </table> |
| - | <table> | + | == Function == |
| + | [https://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]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d5/3d5j_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d5/3d5j_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
| - | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3d5j ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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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> | ||
| + | <div class="pdbe-citations 3d5j" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
| - | [[Category: Barcena | + | [[Category: Barcena JA]] |
| - | [[Category: Discola | + | [[Category: Discola KF]] |
| - | [[Category: Guimaraes | + | [[Category: Guimaraes BG]] |
| - | [[Category: Netto | + | [[Category: Netto LES]] |
| - | + | [[Category: Padilla CA]] | |
| - | [[Category: Padilla | + | [[Category: Porras P]] |
| - | [[Category: Porras | + | [[Category: De Oliveira MA]] |
| - | [[Category: | + | |
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Current revision
Structure of yeast Grx2-C30S mutant with glutathionyl mixed disulfide
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