3rhc: Difference between revisions
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==Crystal structure of the holo form of glutaredoxin C5 from Arabidopsis thaliana== | ==Crystal structure of the holo form of glutaredoxin C5 from Arabidopsis thaliana== | ||
<StructureSection load='3rhc' size='340' side='right' caption='[[3rhc]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='3rhc' size='340' side='right' caption='[[3rhc]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3rhc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3rhc]] is a 2 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=3RHC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RHC FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</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"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3fz9|3fz9]], [[3rhb|3rhb]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3fz9|3fz9]], [[3rhb|3rhb]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GRXC5, At4g28730, F16A16.160 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GRXC5, At4g28730, F16A16.160 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</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=3rhc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rhc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rhc RCSB], [http://www.ebi.ac.uk/pdbsum/3rhc 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=3rhc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rhc OCA], [http://pdbe.org/3rhc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3rhc RCSB], [http://www.ebi.ac.uk/pdbsum/3rhc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3rhc ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/GRXC5_ARATH GRXC5_ARATH]] Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins. Can assemble a [2Fe-2S] cluster, but cannot transfer it to an apoferredoxin.<ref>PMID:21632542</ref> | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3rhc" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Arath]] | ||
[[Category: Couturier, J]] | [[Category: Couturier, J]] | ||
[[Category: Didierjean, C]] | [[Category: Didierjean, C]] | ||
Revision as of 23:24, 11 August 2016
Crystal structure of the holo form of glutaredoxin C5 from Arabidopsis thalianaCrystal structure of the holo form of glutaredoxin C5 from Arabidopsis thaliana
Structural highlights
Function[GRXC5_ARATH] Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins. Can assemble a [2Fe-2S] cluster, but cannot transfer it to an apoferredoxin.[1] Publication Abstract from PubMedUnlike thioredoxins, glutaredoxins are involved in iron-sulfur cluster assembly and in reduction of specific disulfides i.e. protein-glutathione adducts, and thus they are also important redox regulators of chloroplast metabolism. Using GFP fusion, AtGrxC5 isoform, present exclusively in Brassicaceae, is shown to be localized in chloroplasts. A comparison of the biochemical, structural and spectroscopic properties of Arabidopsis GrxC5 (WCSYC active site) with poplar GrxS12 (WCSYS active site), a chloroplastic paralog, indicates that, contrary to the solely apomonomeric GrxS12 isoform, AtGrxC5 exists as two forms when expressed in Escherichia coli. The monomeric apoprotein possesses deglutathionylation activity mediating the recycling of plastidial methionine sulfoxide reductase B1 and peroxiredoxin IIE, whereas the dimeric holoprotein incorporates a [2Fe-2S] cluster. Site-directed mutagenesis experiments and resolution of the X-ray crystal structure of AtGrxC5 in its holoform revealed that, although not involved in its ligation, the presence of the second active site cysteine (Cys32) is required for cluster formation. In addition, thiol titrations, fluorescence measurements and mass spectrometry analyses show that, despite the presence of a dithiol active site, AtGrxC5 does not form any inter- or intramolecular disulfide bond and that its activity exclusively relies on a monothiol mechanism. Arabidopsis chloroplastic glutaredoxin C5 as a model to explore the molecular determinants for iron-sulfur cluster binding into glutaredoxins.,Couturier J, Stroher E, Albetel AN, Roret T, Muthuramalingam M, Tarrago L, Seidel T, Tsan P, Jacquot JP, Johnson MK, Dietz KJ, Didierjean C, Rouhier N J Biol Chem. 2011 Jun 1. PMID:21632542[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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