Glutathione reductase and thioredoxin reductase at the crossroad: the structure of Schistosoma mansoni thioredoxin glutathione reductase.
Proteins
; 72(3): 936-45, 2008 Aug 15.
Article
in En
| MEDLINE
| ID: mdl-18300227
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.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Schistosoma mansoni
/
Thioredoxin-Disulfide Reductase
/
Glutathione Reductase
/
Multienzyme Complexes
/
NADH, NADPH Oxidoreductases
Limits:
Animals
/
Humans
Language:
En
Journal:
Proteins
Journal subject:
BIOQUIMICA
Year:
2008
Document type:
Article
Affiliation country:
Italy