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Model for the ATP-dependent conformational change in group II chaperonins. Only one ring is shown. A, I, E, and H represent the apical domain, intermediate domain, equatorial domain, and the helical protrusion, respectively. The top view of the crystal structure of Thermococcus sp. strain KS-1 (T. KS-1) chaperonin in the closed conformation is shown with the helical protrusions in the CPK model.
