7ncv
From Proteopedia
(Difference between revisions)
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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'> | + | <table><tr><td colspan='2'>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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</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='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='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='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;"> | ||
| - | == 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<ref>PMID:34069657</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 7ncv" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Chlamydomonas reinhardtii]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Didierjean C]] | [[Category: Didierjean C]] | ||
[[Category: Roret T]] | [[Category: Roret T]] | ||
Current revision
Crystal structure of reduced glutaredoxin 2 from Chlamydomonas reinhardtii
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