HSP60 Protein, Human (His-GST)

HSP60 protein serves as a chaperonin with pivotal roles in mitochondrial protein import and macromolecular assembly. Collaborating with Hsp10, it facilitates the accurate folding of imported proteins and, under stress conditions in the mitochondrial matrix, may prevent misfolding while promoting the refolding and proper assembly of unfolded polypeptides. The structural units of these chaperonins comprise heptameric rings of the large subunit Hsp60, forming a back-to-back double ring. In a cyclic process, Hsp60 ring complexes sequentially bind one unfolded substrate protein per ring, followed by ATP binding and association with two heptameric rings of the co-chaperonin Hsp10. This cyclic interaction leads to the sequestration of the substrate protein within the inner cavity of Hsp60, allowing it to fold undisturbed by other cell components for a certain period. The synchronized hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings, leading to the release of ADP and the properly folded substrate protein (Probable).