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Authored: Matthews, L, 2008-12-01 04:46:41, Edited: Matthews, L, 2009-02-21 05:37:28, Reviewed: Cowan, NJ, 2009-01-21 16:47:24, TriC/CCT-mediated beta-actin folding involves rapid ATP-independent formation of a binary complex, followed by a slower ATP-dependent release of the native product (Gao et al., 1992). Group II chaperonins enclose substrate proteins following substrate binding through the formation of a "built- in" lid over the central cavity. Upon ATP binding, lid formation is triggered by the transition state of ATP hydrolysis (Meyer, et al., 2003).
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Hydrolysis of ATP and release of folded actin from CCT/TriC
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