Source:http://www.reactome.org/biopax/48887BiochemicalReaction1904
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Authored: Matthews, L, 2008-12-01 04:46:41,
Edited: Matthews, L, 2009-02-21 05:37:28,
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). In the case of CCT-mediated tubulin folding, one or more rounds of ATP hydrolysis are likely required before the association of non-exchangeable GTP with chaperonin-bound alpha tubulin.,
Reviewed: Cowan, NJ, 2009-01-21 16:47:24
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Hydrolysis of ATP and release of tubulin folding intermediate from CCT/TriC
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