Redox-dependent domain rearrangement of protein disulfide isomerase from a thermophilic fungus

Redox-dependent conformational and solvation changes of protein disulfide isomerase (PDI) from a thermophilic fungus are studied by using small-angle X-ray scattering (SAXS) analysis. The results have shown that the conformation of PDI is controlled by the redox state of the active site cysteine residues in the thioredoxin a and a' domains and that the conformational alternation has accompanied solvation changes in the active site cleft formed by the thioredoxin a, b, b' and a' domains.