Cloned (Comment) | Organism |
---|---|
expression of residues 23-522 of PDI1 | Saccharomyces cerevisiae |
Crystallization (Comment) | Organism |
---|---|
purified recombinant residues 23-522 of PDI1, X-ray diffraction structure determination and analysis at 2.4 A resolution, modeling | Saccharomyces cerevisiae |
Protein Variants | Comment | Organism |
---|---|---|
C409A | site-directed mutagenesis, mutation of the second cysteine of the active site, the mutant shows similar activity to the wild-type enzyme | Saccharomyces cerevisiae |
C64A | site-directed mutagenesis, mutation of the second cysteine of the active site, the mutant shows similar activity to the wild-type enzyme | Saccharomyces cerevisiae |
additional information | a domain a'-deletion mutant shows reduced activity in refolding of RNase compared to the wild-type enzyme | Saccharomyces cerevisiae |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Saccharomyces cerevisiae | PDI plays a key role in catalyzing the folding of secretory proteins | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
catalyses the rearrangement of -S-S- bonds in proteins | active site location, structure, and redox state | Saccharomyces cerevisiae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | PDI plays a key role in catalyzing the folding of secretory proteins | Saccharomyces cerevisiae | ? | - |
? | |
additional information | all 5 domains of PDI are required for full catalytic activity | Saccharomyces cerevisiae | ? | - |
? | |
RNase | refolding of RNase, renaturation of reduced and of scrambled RNase with almost equal activity | Saccharomyces cerevisiae | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | domain arrangement: two catalytically inactive thioredoxin domains inserted between two catalytically active thioredoxin domains and an acidic C-terminal tail, the four thioredoxin domains form the shape of a twisted U with the active sites facing each other across the long sides, the inside surface is enriched in hydrophobic residues facilitating interactions with misfolded proteins, all 5 domains of PDI are required for full catalytic activity | Saccharomyces cerevisiae |
Synonyms | Comment | Organism |
---|---|---|
PDI | - |
Saccharomyces cerevisiae |
protein disulfide isomerase | - |
Saccharomyces cerevisiae |