2m80
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2m80]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M80 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M80 FirstGlance]. <br> | <table><tr><td colspan='2'>[[2m80]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M80 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M80 FirstGlance]. <br> | ||
| - | </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=2m80 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m80 OCA], [https://pdbe.org/2m80 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m80 RCSB], [https://www.ebi.ac.uk/pdbsum/2m80 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m80 ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2m80 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m80 OCA], [https://pdbe.org/2m80 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m80 RCSB], [https://www.ebi.ac.uk/pdbsum/2m80 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m80 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/GLRX8_YEAST GLRX8_YEAST] Glutathione-dependent oxidoreductase with lower activity compared to the other members of the glutaredoxin family. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase.<ref>PMID:18400945</ref> <ref>PMID:19166312</ref> | [https://www.uniprot.org/uniprot/GLRX8_YEAST GLRX8_YEAST] Glutathione-dependent oxidoreductase with lower activity compared to the other members of the glutaredoxin family. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase.<ref>PMID:18400945</ref> <ref>PMID:19166312</ref> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Glutaredoxins (Grxs) are wide-spread oxidoreductases that are found in all kingdoms of life. The yeast Saccharomyces cerevisiae encodes eight Grxs, among which, Grx8 shares a sequence identity of 30 and 23% with typical dithiol Grx1 and Grx2, respectively, but it exhibits a much lower GSH-dependent oxidoreductase activity. To elucidate its catalytic mechanism, we solved the solution structure of Grx8, which displays a typical Grx fold. Structural analysis indicated that Grx8 possesses a negatively charged CXXC motif (Cys(33)-Pro(34)-Asp(35)-Cys(36)) and a GSH-recognition site, which are distinct from Grx1 and Grx2. Subsequent structure-guided site mutations revealed that the D35Y single mutant and N80T/L81V double mutant possess increased activity of 10- and 11-fold, respectively; moreover, the D35Y/N80T/L81V triple mutant has increased activity of up to 44-fold, which is comparable to that of canonical Grx. Biochemical analyses suggested that the increase in catalytic efficiency resulted from a decreased pKa value of catalytic cysteine Cys33 and/or enhancement of the putative GSH-recognition site. Moreover, NMR chemical shift perturbation analyses combined with GSH analogue inhibition assays enabled us to elucidate that wild-type Grx8 and all mutants adopt a ping-pong mechanism of catalysis. All together, these findings provide structural insights into the catalytic mechanism of dithiol Grxs. | ||
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| - | Structure-guided activity enhancement and catalytic mechanism of yeast grx8.,Tang Y, Zhang J, Yu J, Xu L, Wu J, Zhou CZ, Shi Y Biochemistry. 2014 Apr 8;53(13):2185-96. doi: 10.1021/bi401293s. Epub 2014 Mar, 25. PMID:24611845<ref>PMID:24611845</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 2m80" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Solution structure of yeast dithiol glutaredoxin Grx8
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Categories: Large Structures | Saccharomyces cerevisiae S288C | Shi Y | Tang Y | Wu J | Yu J | Zhang J | Zhou CZ
