2lv3: Difference between revisions
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==Structure-functional characterization of Grx domain of Mus musculus TGR== | |||
<StructureSection load='2lv3' size='340' side='right' caption='[[2lv3]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2lv3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LV3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LV3 FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3h8q|3h8q]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Tgr ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thioredoxin-disulfide_reductase Thioredoxin-disulfide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.9 1.8.1.9] </span></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=2lv3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lv3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lv3 RCSB], [http://www.ebi.ac.uk/pdbsum/2lv3 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Thioredoxin glutathione reductase (TGR) is a member of the mammalian thioredoxin reductase family that has a monothiol glutaredoxin (Grx) domain attached to the thioredoxin reductase module. Here, we report a structure of the Grx domain of mouse TGR, determined through high resolution NMR spectroscopy to the final backbone RMSD value of 0.48 +/- 0.10 A. The structure represents a sandwich-like molecule composed of a four stranded beta-sheet flanked by five alpha-helixes, with the CxxS active motif located on the catalytic loop. We structurally characterized the glutathione-binding site in the protein and describe sequence and structural relationships of the domain with glutaredoxins. The structure illuminates a key functional center that evolved in mammalian TGRs to act in thiol-disulfide reactions. Our study allows us to hypothesize that Cys105 might be functionally relevant for TGR catalysis. In addition, the data suggest that the N-terminus of Grx acts as a possible regulatory signal also protecting the protein active site from unwanted interactions in cellular cytosol. | |||
Structural analysis of glutaredoxin domain of Mus musculus thioredoxin glutathione reductase.,Dobrovolska O, Shumilina E, Gladyshev VN, Dikiy A PLoS One. 2012;7(12):e52914. doi: 10.1371/journal.pone.0052914. Epub 2012 Dec 26. PMID:23300818<ref>PMID:23300818</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== | ==See Also== | ||
*[[Thioredoxin Reductase|Thioredoxin Reductase]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Thioredoxin-disulfide reductase]] | [[Category: Thioredoxin-disulfide reductase]] | ||
[[Category: Dikiy, A | [[Category: Dikiy, A]] | ||
[[Category: Dobrovolska, O | [[Category: Dobrovolska, O]] | ||
[[Category: Gladyshev, V | [[Category: Gladyshev, V]] | ||
[[Category: Shumilina, E | [[Category: Shumilina, E]] | ||
[[Category: Grx]] | [[Category: Grx]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
[[Category: Tgr]] | [[Category: Tgr]] | ||
Revision as of 12:31, 18 December 2014
Structure-functional characterization of Grx domain of Mus musculus TGR
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