DSBC protein: a new member of the thioredoxin fold-containing family.
Prediction of the DsbC protein secondary structure has been performed using a novel prediction technique which is based on consideration of both local and long-range interactions between amino acid residues. The C-terminal portion of the protein is shown to contain the thioredoxin folding motif. The N-terminal part represents a yet unknown structural domain.
Frishman
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European Molecular Biology Laboratory, Heidelberg, Germany.
D000595:Amino Acid Sequence; D001665:Binding Sites; D004220:Disulfides; D004885:Erwinia / Q000201:enzymology; D004926:Escherichia coli / Q000201:enzymology; D005979:Glutathione Peroxidase / Q000737:chemistry; D005982:Glutathione Transferase / Q000737:chemistry; D007535:Isomerases / Q000737:chemistry*; D008961:Models, Structural; D008969:Molecular Sequence Data; D019704:Protein Disulfide-Isomerases; D017433:Protein Structure, Secondary; D017386:Sequence Homology, Amino Acid
D004220:Disulfides; D005979:Glutathione Peroxidase; D005982:Glutathione Transferase; D007535:Isomerases; D019704:Protein Disulfide-Isomerases