Protein disulfide-isomerase has two catalytic thioredoxin-like domains (active sites), each containing the canonical CGHC motif, and two non catalytic domains.
This structure is similar to the structure of enzymes responsible for oxidative folding in the intermembrane space of the mitochondria; an example of this is mitochondrial IMS import and assembly (Mia40), which has 2 catalytic domains that contain a CX₉C, which is similar to the CGHC domain of PDI.
Bacterial DsbA, responsible for oxidative folding, also has a thioredoxin CXXC domain.
Protein disulfide-isomerase has two catalytic thioredoxin-like domains (active sites), each containing the canonical CGHC motif, and two non catalytic domains. This structure is similar to the structure of enzymes responsible for oxidative folding in the intermembrane space of the mitochondria; an example of this is mitochondrial IMS import and assembly (Mia40), which has 2 catalytic domains that contain a CX₉C, which is similar to the CGHC domain of PDI. Bacterial DsbA, responsible for oxidative folding, also has a thioredoxin CXXC domain.
Protein disulfide-isomerase