Chemical shift assignments of a reduced N-terminal truncation mutant of the disulfide bond isomerase TrbB from plasmid F, TrbBΔ29.
TrbB from the conjugative plasmid F is a 181-residue disulfide bond isomerase that plays a role in the correct folding and maintenance of disulfide bonds within F plasmid encoded proteins in the bacterial periplasm. As a member of the thioredoxin-like superfamily, TrbB has a predicted thioredoxin-like fold that contains a C-X-X-C active site required for performing specific redox chemistries on protein substrates. Here we report the sequence-specific assignments of the reduced form of the N-terminally truncated TrbB construct, TrbBΔ29.
Department of Biology, The Johns Hopkins University, Baltimore, MD, 21218, USA.
Casey W
CW
Hemmis
Nathan T
NT
Wright
Ananya
A
Majumdar
Joel F
JF
Schildbach
D000595:Amino Acid Sequence; D005144:F Factor / Q000235:genetics*; D019906:Nuclear Magnetic Resonance, Biomolecular; D019704:Protein Disulfide-Isomerases / Q000737:chemistry* / Q000235:genetics*; D017384:Sequence Deletion
D019704:Protein Disulfide-Isomerases