2LV3

Structure-functional characterization of Grx domain of Mus musculus TGR

Summary for 2LV3

• Entry DOI: 10.2210/pdb2lv3/pdb
• Related: 3H8Q
• NMR Information: BMRB: 17636
• Descriptor: Thioredoxin reductase 3 (1 entity in total)
• Functional Keywords: grx, tgr, oxidoreductase
• Biological source: Mus musculus (mouse)
• Cellular location: Cytoplasm : Q99MD6
• Total number of polymer chains: 1
• Total formula weight: 13371.11

Authors

Dobrovolska, O.,Shumilina, E.,Gladyshev, V.,Dikiy, A. (deposition date: 2012-06-28, release date: 2013-05-22, Last modification date: 2024-05-15)

Primary citation

Dobrovolska, O.,Shumilina, E.,Gladyshev, V.N.,Dikiy, A.
Structural analysis of glutaredoxin domain of Mus musculus thioredoxin glutathione reductase
Plos One, 7:e52914-e52914, 2012

PubMed 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.

PubMed: 23300818
DOI: 10.1371/journal.pone.0052914

Experimental method

SOLUTION NMR