3c1s: Difference between revisions

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==Crystal structure of GRX1 in glutathionylated form==
==Crystal structure of GRX1 in glutathionylated form==
<StructureSection load='3c1s' size='340' side='right' caption='[[3c1s]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='3c1s' size='340' side='right'caption='[[3c1s]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3c1s]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C1S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3C1S FirstGlance]. <br>
<table><tr><td colspan='2'>[[3c1s]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C1S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3C1S FirstGlance]. <br>
</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>
</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 id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3c1r|3c1r]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3c1r|3c1r]]</div></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GRX1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GRX1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Arsenate_reductase_(glutaredoxin) Arsenate reductase (glutaredoxin)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.20.4.1 1.20.4.1] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Arsenate_reductase_(glutaredoxin) Arsenate reductase (glutaredoxin)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.20.4.1 1.20.4.1] </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=3c1s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c1s OCA], [http://pdbe.org/3c1s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3c1s RCSB], [http://www.ebi.ac.uk/pdbsum/3c1s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3c1s 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=3c1s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c1s OCA], [https://pdbe.org/3c1s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3c1s RCSB], [https://www.ebi.ac.uk/pdbsum/3c1s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3c1s ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/GLRX1_YEAST GLRX1_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>   
[[https://www.uniprot.org/uniprot/GLRX1_YEAST GLRX1_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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</StructureSection>
</StructureSection>
[[Category: Atcc 18824]]
[[Category: Atcc 18824]]
[[Category: Large Structures]]
[[Category: Yu, J]]
[[Category: Yu, J]]
[[Category: Zhou, C Z]]
[[Category: Zhou, C Z]]
[[Category: Glutathionylated form]]
[[Category: Glutathionylated form]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]

Revision as of 07:39, 27 January 2022

Crystal structure of GRX1 in glutathionylated form

3c1s, resolution 2.50Å

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