2V6O
Structure of Schistosoma mansoni Thioredoxin-Glutathione Reductase (SmTGR)
Summary for 2V6O
| Entry DOI | 10.2210/pdb2v6o/pdb |
| Descriptor | THIOREDOXIN GLUTATHIONE REDUCTASE, FLAVIN-ADENINE DINUCLEOTIDE, TETRAETHYLENE GLYCOL, ... (5 entities in total) |
| Functional Keywords | fad, flavoprotein, oxidoreductase, chimeric enzyme, thiol-mediated detoxification pathway, redox-active center |
| Biological source | SCHISTOSOMA MANSONI (BLOOD FLUKE) |
| Total number of polymer chains | 1 |
| Total formula weight | 66525.41 |
| Authors | Miele, A.E.,Angelucci, F.,Boumis, G.,Dimastrogiovanni, D.,Bellelli, A.,Brunori, M. (deposition date: 2007-07-19, release date: 2008-03-04, Last modification date: 2024-10-23) |
| Primary citation | Angelucci, F.,Miele, A.E.,Boumis, G.,Dimastrogiovanni, D.,Brunori, M.,Bellelli, A. Glutathione Reductase and Thioredoxin Reductase at the Crossroad: The Structure of Schistosoma Mansoni Thioredoxin Glutathione Reductase Proteins, 72:936-, 2008 Cited by PubMed Abstract: Thioredoxin glutathione reductase (TGR) is a key flavoenzyme expressed by schistosomes that bridges two detoxification pathways crucial for the parasite survival in the host's organism. In this article we report the crystal structure (at 2.2 A resolution) of TGR from Schistosoma mansoni (SmTGR), deleted in the last two residues. The structure reveals the peculiar architecture of this chimeric enzyme: the small Glutaredoxin (Grx) domain at the N-terminus is joined to the large thioredoxin reductase (TR) one via an extended complementary surface, involving residues not conserved in the Grx superfamily; the TR domain interacts with an identical partner via its C-terminal domain, forming a dimer with a twisted "W" shape. Although lacking the penultimate Selenocysteine residue (Sec), the enzyme is still able to reduce oxidized glutathione. These data update the interpretation of the interdomain communication in TGR enzymes. The possible function of this enzyme in pathogenic parasites is discussed. PubMed: 18300227DOI: 10.1002/PROT.21986 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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