RelevanceGroEL and GroES are E.coli chaperones, which are homologs of the mitochondrial chaperones Hsp60 and Hsp10 respectively. GroEL is a double toriodal assembly of 14 identical subunits which form two heptameric rings stacked back-to-back, with a cavity at each end. GroEL and its co-chaperonin GroES facilitate protein folding in an ATP-dependent mechanism. Binding of substrate protein, in addition to binding of ATP, induces a conformational change that allows association of this binary complex with a separate lid structure, GroES.
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