A Structural Disulfide of Yeast Protein-disulfide Isomerase Destabilizes the Active Site Disulfide of the N-terminal Thioredoxin Domain

PROBING THE ACTIVE SITE OF RHODANESE WITH DISULFIDE REAGENTS

probing the active site of rhodanese with disulfide reagents

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The folding catalyst protein disulfide isomerase is constructed of active and inactive thioredoxin modules

BACKGROUND Protein disulfide isomerase (PDI), a multifunctional protein of the endoplasmic reticulum, catalyzes the formation, breakage and rearrangement of disulfide bonds during protein folding. Dissection of this protein into its individual domains has confirmed the presence of the a and a' domains, which are homologous to thioredoxin, having related structures and activities. The a and a' d...

The acidic C-terminal domain stabilizes the chaperone function of protein disulfide isomerase.

Protein disulfide isomerase (PDI, EC 5.3.4.1) is a chaperone and catalyzes the formation and rearrangement of disulfide bonds in proteins. Domain c-(463-491), containing 18 acidic residues, is an interesting and important C-terminal extension of PDI. In this study, the PDI mutant abb'a', in which domain c is truncated, was used to investigate the relationship between the C-terminal structure an...

Development of a Novel Anti-Adhesive Vaccine Against Pseudomonas aeruginosa Targeting the C-terminal Disulfide Loop of the Pilin Protein

The type IV pili (T4P) is a major virulence factor of Pseudomonas aeruginosa (P. aeruginosa) that is associated with primary adhesion, biofilm formation and twitching motility. This study focuses on the introduction of a novel biologically active subunit vaccine derived from the disulfide loop (DSL) of P. aeruginosa pilin. We investigated the expression of the novel PilA in-frame with pET26a ve...