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Structural Analysis of Glutaredoxin Domain of Mus musculus Thioredoxin Glutathione Reductase

Authors
Journal
PLoS ONE
1932-6203
Publisher
Public Library of Science
Publication Date
Volume
7
Issue
12
Identifiers
DOI: 10.1371/journal.pone.0052914
Keywords
  • Research Article
  • Biology
  • Biochemistry
  • Proteins
  • Protein Structure
  • Enzymes
  • Biophysics
  • Computational Biology
  • Macromolecular Structure Analysis
  • Sequence Analysis
  • Proteomics
  • Spectrometric Identification Of Proteins
Disciplines
  • Biology

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.

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