Structural Analysis of Glutaredoxin Domain of Mus Musculus Thioredoxin Glutathione Reductase

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Structural Analysis of Glutaredoxin Domain of Mus Musculus Thioredoxin Glutathione Reductase

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Title: Structural Analysis of Glutaredoxin Domain of Mus Musculus Thioredoxin Glutathione Reductase
Author: Dobrovolska, Olena; Shumilina, Elena; Gladyshev, Vadim; Dikiy, Alexander

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Citation: Dobrovolska, Olena, Elena Shumilina, Vadim N. Gladyshev, and Alexander Dikiy. 2012. Structural analysis of glutaredoxin domain of mus musculus thioredoxin glutathione reductase. PLoS ONE 7(12): e52914.
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Abstract: 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 Å. The structure represents a sandwich-like molecule composed of a four stranded β-sheet flanked by five α–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.
Published Version: doi:10.1371/journal.pone.0052914
Other Sources: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3530482/pdf/
Terms of Use: This article is made available under the terms and conditions applicable to Other Posted Material, as set forth at http://nrs.harvard.edu/urn-3:HUL.InstRepos:dash.current.terms-of-use#LAA
Citable link to this page: http://nrs.harvard.edu/urn-3:HUL.InstRepos:11181099
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