[HTML][HTML] Glutaredoxin-3 from Escherichia coli: amino acid sequence, 1H and 15N NMR assignments, and structural analysis (∗)
F Åslund, K Nordstrand, KD Berndt, M Nikkola… - Journal of Biological …, 1996 - ASBMB
The primary and secondary structure of glutaredoxin-3 (Grx3), a glutathione-disulfide
oxidoreductase from Escherichia coli, has been determined. The amino acid sequence of
Grx3 consists of 82 residues and contains a redox-active motif, Cys-Pro-Tyr-Cys, typical of
the glutaredoxin family. Sequence comparison reveals a homology (33% identity) to that of
glutaredoxin-1 (Grx1) from E. coli as well as to other members of the thioredoxin superfamily.
In addition to the active site cysteine residues, Grx3 contains one additional cysteine (Cys …
oxidoreductase from Escherichia coli, has been determined. The amino acid sequence of
Grx3 consists of 82 residues and contains a redox-active motif, Cys-Pro-Tyr-Cys, typical of
the glutaredoxin family. Sequence comparison reveals a homology (33% identity) to that of
glutaredoxin-1 (Grx1) from E. coli as well as to other members of the thioredoxin superfamily.
In addition to the active site cysteine residues, Grx3 contains one additional cysteine (Cys …
