Structural basis for the thioredoxin-like activity profile of the glutaredoxin-like NrdH-redoxin from Escherichia coli.

@article{Stehr2001StructuralBF,
  title={Structural basis for the thioredoxin-like activity profile of the glutaredoxin-like NrdH-redoxin from Escherichia coli.},
  author={Matthias Stehr and G. R. Eugenia Schneider and Fredrik {\AA}slund and Arne Holmgren and Ylva Lindqvist},
  journal={The Journal of biological chemistry},
  year={2001},
  volume={276 38},
  pages={35836-41}
}
NrdH-redoxin is a representative of a class of small redox proteins that contain a conserved CXXC motif and are characterized by a glutaredoxin-like amino acid sequence and thioredoxin-like activity profile. The crystal structure of recombinant Escherichia coli NrdH-redoxin in the oxidized state has been determined at 1.7 A resolution by multiwavelength anomalous diffraction. NrdH-redoxin belongs to the thioredoxin superfamily and is structurally most similar to E. coli glutaredoxin 3 and phage… CONTINUE READING
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