page_title: Protein disulfide-isomerase
section_title: Structure
hierarchical_section_title: Protein disulfide-isomerase / Structure
caption_attribution_description: English: Primary structure of protein disulfide isomerase
context_page_description: Protein disulfide isomerase, or PDI, is an enzyme in the endoplasmic reticulum in eukaryotes and the periplasm of bacteria that catalyzes the formation and breakage of disulfide bonds between cysteine residues within proteins as they fold. This allows proteins to quickly find the correct arrangement of disulfide bonds in their fully folded state, and therefore the enzyme acts to catalyze protein folding.
context_section_description: 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.
caption: Primary structure of protein disulfide isomerase with sequence of domains
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