1). DsbA has a thioredoxin domain and an α-helical domain insertion [6], the former of which contains the redox active-site sequence, Cys30–Pro31–His32–Cys33, which has the highest redox potential value (∼− 120 mV) among all the known thiol–disulfide oxido-reductases [7], ...
The X-ray crystal structure of Mt-DsbA reveals a two-domain structure, comprising a canonical thioredoxin domain with the conserved CXXC active site cysteines in their reduced form, and an inserted α-helical domain containing a structural disulfide bond. The overall fold of Mt-DsbA resembles ...
The X-ray crystal structure of Mt-DsbA reveals a two-domain structure, comprising a canonical thioredoxin domain with the conserved CXXC active site cysteines in their reduced form, and an inserted ??-helical domain containing a structural disulfide bond. The overall fold of Mt-DsbA resembles ...
Residues comprising the thioredoxin domain of EcDsbA are underlined. Residues that make contacts to the peptide substrate in the crystal structure of the complex are highlighted (*). b–e, phenotypic assays on dsbA− E. coli (JCB571) complemented with different DsbA proteins. b, JCB571 alone...
The disulfide oxidoreductase DsbA is a strong oxidant of protein thiols and required for efficient disulfide bond formation in the bacterial periplasm. The enzyme consists of a thioredoxin-like domain and a second, alpha-helical domain which is inserted
The crystal structure of Rv2969c reveals a canonical DsbA fold comprising a thioredoxin domain with an embedded helical domain. However, Rv2969c diverges considerably from other DsbAs, including having an additional C‐terminal helix (H8) that may restrain the mobility of the catalytic helix H1....
The structure of DsbA is comprised of a thioredoxin domain with an inserted helical domain [9,10,11]. Like many other thiol-disulfide oxidoreductase enzymes, the active site of DsbA is comprised of the characteristic CXXC motif (Cys30–Pro31–His32–Cys33 in Escherichia coli DsbA) and a ...