2m80: Difference between revisions

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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.
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>
From MEDLINE&reg;/PubMed&reg;, 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/>

Latest revision as of 09:59, 1 May 2024

Solution structure of yeast dithiol glutaredoxin Grx8Solution structure of yeast dithiol glutaredoxin Grx8

Structural highlights

2m80 is a 1 chain structure with sequence from Saccharomyces cerevisiae S288C. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.[1] [2]

References

  1. ↑ Mesecke N, Spang A, Deponte M, Herrmann JM. A novel group of glutaredoxins in the cis-Golgi critical for oxidative stress resistance. Mol Biol Cell. 2008 Jun;19(6):2673-80. doi: 10.1091/mbc.E07-09-0896. Epub 2008, Apr 9. PMID:18400945 doi:http://dx.doi.org/10.1091/mbc.E07-09-0896
  2. ↑ Eckers E, Bien M, Stroobant V, Herrmann JM, Deponte M. Biochemical characterization of dithiol glutaredoxin 8 from Saccharomyces cerevisiae: the catalytic redox mechanism redux. Biochemistry. 2009 Feb 17;48(6):1410-23. doi: 10.1021/bi801859b. PMID:19166312 doi:http://dx.doi.org/10.1021/bi801859b
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