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| | <StructureSection load='5y4u' size='340' side='right'caption='[[5y4u]], [[Resolution|resolution]] 1.70Å' scene=''> | | <StructureSection load='5y4u' size='340' side='right'caption='[[5y4u]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5y4u]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y4U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Y4U FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5y4u]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y4U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5Y4U FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GRX3, YDR098C, YD8557.05C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</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]] 1.7Å</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=5y4u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y4u OCA], [http://pdbe.org/5y4u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5y4u RCSB], [http://www.ebi.ac.uk/pdbsum/5y4u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5y4u 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=5y4u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y4u OCA], [https://pdbe.org/5y4u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5y4u RCSB], [https://www.ebi.ac.uk/pdbsum/5y4u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5y4u ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GLRX3_YEAST GLRX3_YEAST]] Monothiol glutaredoxin involved in the biogenesis of iron-sulfur clusters (By similarity). Binds one iron-sulfur cluster per dimer. The iron-sulfur cluster is bound between subunits, and is complexed by a bound glutathione and a cysteine residue from each subunit (Probable). | + | [https://www.uniprot.org/uniprot/GLRX3_YEAST GLRX3_YEAST] Monothiol glutaredoxin involved in the biogenesis of iron-sulfur clusters (By similarity). Binds one iron-sulfur cluster per dimer. The iron-sulfur cluster is bound between subunits, and is complexed by a bound glutathione and a cysteine residue from each subunit (Probable). |
| | <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: Baker's yeast]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Abdalla, M]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Chen, Y X]] | + | [[Category: Abdalla M]] |
| - | [[Category: Chi, C B]] | + | [[Category: Chen YX]] |
| - | [[Category: Dai, Y N]] | + | [[Category: Chi CB]] |
| - | [[Category: Tang, Y J]] | + | [[Category: Dai YN]] |
| - | [[Category: Zhang, J H]] | + | [[Category: Tang YJ]] |
| - | [[Category: Zhou, C Z]] | + | [[Category: Zhang JH]] |
| - | [[Category: Glutathione]]
| + | [[Category: Zhou CZ]] |
| - | [[Category: Monothiol glutaredoxin]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
GLRX3_YEAST Monothiol glutaredoxin involved in the biogenesis of iron-sulfur clusters (By similarity). Binds one iron-sulfur cluster per dimer. The iron-sulfur cluster is bound between subunits, and is complexed by a bound glutathione and a cysteine residue from each subunit (Probable).
Publication Abstract from PubMed
The yeast Saccharomyces cerevisiae monothiol glutaredoxin Grx3 plays a key role in cellular defense against oxidative stress and more importantly, cooperates with BolA-like iron repressor of activation protein Fra2 to regulate the localization of the iron-sensing transcription factor Aft2. The interplay among Grx3, Fra2 and Aft2 responsible for the regulation of iron homeostasis has not been clearly described. Here we solved the crystal structures of the Trx domain (Grx3(Trx)) and Grx domain (Grx3(Grx)) of Grx3 in addition to the solution structure of Fra2. Structural analyses and activity assays indicated that the Trx domain also contributes to the glutathione S-transferase activity of Grx3, via an inter-domain disulfide bond between Cys37 and Cys176. NMR titration and pull-down assays combined with surface plasmon resonance experiments revealed that Fra2 could form a noncovalent heterodimer with Grx3 via an interface between the helix-turn-helix motif of Fra2 and the C-terminal segment of Grx3(Grx), different from the previously identified covalent heterodimer mediated by Fe-S cluster. Comparative affinity assays indicated that the interaction between Fra2 and Aft2 is much stronger than that between Grx3 and Aft2, or Aft2 toward its target DNA. These structural and biochemical analyses enabled us to propose a model how Grx3 executes multiple functions to coordinate the regulation of Aft2-controlled iron metabolism.
Structural and Biochemical Insights into the Multiple Functions of Yeast Grx3.,Chi CB, Tang Y, Zhang J, Dai YN, Abdalla M, Chen Y, Zhou CZ J Mol Biol. 2018 Mar 7. pii: S0022-2836(18)30110-4. doi:, 10.1016/j.jmb.2018.02.024. PMID:29524511[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chi CB, Tang Y, Zhang J, Dai YN, Abdalla M, Chen Y, Zhou CZ. Structural and Biochemical Insights into the Multiple Functions of Yeast Grx3. J Mol Biol. 2018 Mar 7. pii: S0022-2836(18)30110-4. doi:, 10.1016/j.jmb.2018.02.024. PMID:29524511 doi:http://dx.doi.org/10.1016/j.jmb.2018.02.024
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