WebMar 1, 2016 · DsbA harbors a canonical thioredoxin-like fold that is characterized by an N-terminal βαβ motif and a C-terminal ββα motif . However, unlike thioredoxin, these motifs are separated by an extended α-helical domain. ... This thioredoxin-like enzyme is required for the proper folding of secreted proteins with nonconsecutive disulfide bonds ... WebNov 19, 2004 · The search for thioredoxin-like fold proteins in the PDB database identified 723 protein domains. These domains are grouped into eleven evolutionary families based on combined sequence, structural, and functional evidence. Analysis of the protein–ligand structure complexes reveals two major active site locations for the thioredoxin-like …

Thioredoxin - Wikipedia

WebJun 1, 2003 · Sequence homology between members is poor, their relatedness lying in the structural similarity of the thioredoxin-like fold (12). It has been proposed that different PDIs may show different ... WebThioredoxin is a class of small redox proteins known to be present in all organisms. It plays a role in many important ... Thioredoxin proteins also have a characteristic tertiary structure termed the thioredoxin fold. The active site contains a dithiols in a CXXC motif. These two cysteines are the key to the ability of thioredoxin to reduce ... bot international logistics

Structural classification of thioredoxin-like fold proteins

WebReduced thioredoxin also catalyzes the reduction of many exposed disulfides in proteins, thereby functioning as a general protein disulfide-reductase or protein disulfide-isomerase … WebMar 1, 1995 · The thioredoxin fold in situ. The thioredoxin fold comprises about 80 residues, but each of the proteins containing it has extra residues in addition to the fold (Figure 1).Glutaredoxin (87 residues) and thioredoxin (108 residues) are single-domain monomeric proteins: glutaredoxin has little structure in addition to the basic thioredoxin fold, whereas … WebDec 20, 2012 · The structure revealed a thioredoxin-like fold, a β-α-β-β-β-α secondary structure core, and a CXXC motif in an exposed loop in a position similar to the redox-active CXXC site in thioredoxin. Analysis of protein dynamics revealed rigidity in the backbone, except for the 20 residues at the N terminus and 5 residues at the C terminus. ... haydale loughborough