Chaperonin ATPase
Definition:
EC Tree > 5 Isomerases > 5.6 Isomerases altering macromolecular conformation > 5.6.1 Enzymes altering polypeptide conformation or assembly > 5.6.1.7 chaperonin ATPase
Chaperonin ATPase is a multisubunit protein with 2×7 (Type I, most cells) or 2×8 (Type II, Archaea) ATP-binding sites, maintaining unfolded polypeptide structure before folding or mitochondrial/chloroplast import; subunits are 10-90 kDa. It is a subclass of molecular chaperones related to proteasome ATPase. It hydrolyzes ATP to fold an unfolded polypeptide. It appears in viruses and cellular organisms. Structurally it is a GroEL/TRiC chaperonin.
Chaperonin ATPase is a multisubunit protein with 2×7 (Type I, most cells) or 2×8 (Type II, Archaea) ATP-binding sites, maintaining unfolded polypeptide structure before folding or mitochondrial/chloroplast import; subunits are 10-90 kDa. It is a subclass of molecular chaperones related to proteasome ATPase. It hydrolyzes ATP to fold an unfolded polypeptide. It appears in viruses and cellular organisms. Structurally it is a GroEL/TRiC chaperonin.
References:
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