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| | <StructureSection load='7ncv' size='340' side='right'caption='[[7ncv]], [[Resolution|resolution]] 1.50Å' scene=''> | | <StructureSection load='7ncv' size='340' side='right'caption='[[7ncv]], [[Resolution|resolution]] 1.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[7ncv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlre Chlre]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7NCV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7NCV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7ncv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7NCV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7NCV 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=NA:SODIUM+ION'>NA</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]] 1.5Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></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=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GRX2, CHLRE_12g550400v5, CHLREDRAFT_195611 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3055 CHLRE])</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=7ncv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ncv OCA], [https://pdbe.org/7ncv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ncv RCSB], [https://www.ebi.ac.uk/pdbsum/7ncv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ncv 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=7ncv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ncv OCA], [https://pdbe.org/7ncv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ncv RCSB], [https://www.ebi.ac.uk/pdbsum/7ncv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ncv ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A8IYH1_CHLRE A8IYH1_CHLRE] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Chlre]] | + | [[Category: Chlamydomonas reinhardtii]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Didierjean, C]] | + | [[Category: Didierjean C]] |
| - | [[Category: Roret, T]] | + | [[Category: Roret T]] |
| - | [[Category: Chlamydomonas reinhardtii glutaredoxin]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
A8IYH1_CHLRE
Publication Abstract from PubMed
Glutaredoxins (GRXs) are thioredoxin superfamily members exhibiting thiol-disulfide oxidoreductase activity and/or iron-sulfur (Fe-S) cluster binding capacities. These properties are determined by specific structural factors. In this study, we examined the capacity of the class I Chlamydomonas reinhardtii GRX2 recombinant protein to catalyze both protein glutathionylation and deglutathionylation reactions using a redox sensitive fluorescent protein as a model protein substrate. We observed that the catalytic cysteine of the CPYC active site motif of GRX2 was sufficient for catalyzing both reactions in the presence of glutathione. Unexpectedly, spectroscopic characterization of the protein purified under anaerobiosis showed the presence of a [2Fe-2S] cluster despite having a presumably inadequate active site signature, based on past mutational analyses. The spectroscopic characterization of cysteine mutated variants together with modeling of the Fe-S cluster-bound GRX homodimer from the structure of an apo-GRX2 indicate the existence of an atypical Fe-S cluster environment and ligation mode. Overall, the results further delineate the biochemical and structural properties of conventional GRXs, pointing to the existence of multiple factors more complex than anticipated, sustaining the capacity of these proteins to bind Fe-S clusters.
Atypical Iron-Sulfur Cluster Binding, Redox Activity and Structural Properties of Chlamydomonas reinhardtii Glutaredoxin 2.,Roret T, Zhang B, Moseler A, Dhalleine T, Gao XH, Couturier J, Lemaire SD, Didierjean C, Johnson MK, Rouhier N Antioxidants (Basel). 2021 May 19;10(5). pii: antiox10050803. doi:, 10.3390/antiox10050803. PMID:34069657[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Roret T, Zhang B, Moseler A, Dhalleine T, Gao XH, Couturier J, Lemaire SD, Didierjean C, Johnson MK, Rouhier N. Atypical Iron-Sulfur Cluster Binding, Redox Activity and Structural Properties of Chlamydomonas reinhardtii Glutaredoxin 2. Antioxidants (Basel). 2021 May 19;10(5). pii: antiox10050803. doi:, 10.3390/antiox10050803. PMID:34069657 doi:http://dx.doi.org/10.3390/antiox10050803
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