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]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2lv3]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=2LV3 FirstGlance]. <br> | |||
</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=2lv3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lv3 OCA], [https://pdbe.org/2lv3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lv3 RCSB], [https://www.ebi.ac.uk/pdbsum/2lv3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lv3 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/TRXR3_MOUSE TRXR3_MOUSE] Displays thioredoxin reductase, glutaredoxin and glutathione reductase activities. Catalyzes disulfide bond isomerization. Promotes disulfide bond formation between GPX4 and various sperm proteins and may play a role in sperm maturation by promoting formation of sperm structural components.<ref>PMID:11259642</ref> <ref>PMID:15901730</ref> | |||
<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> | |||
<div class="pdbe-citations 2lv3" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Thioredoxin reductase 3D structures|Thioredoxin reductase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | |||
[[Category: Dikiy A]] | |||
[[Category: Dobrovolska O]] | |||
[[Category: Gladyshev V]] | |||
[[Category: Shumilina E]] | |||