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Details on Person Group II chaperonins enclose substrate proteins following su...
| Class:Id | Summation:391885 |
|---|---|
| _displayName | Group II chaperonins enclose substrate proteins following su... |
| _timestamp | 2009-03-08 07:14:05 |
| created | [InstanceEdit:391896] Matthews, L, 2009-02-25 04:39:11 |
| literatureReference | [LiteratureReference:391890] Closing the folding chamber of the eukaryotic chaperonin requires the transition state of ATP hydrolysis |
| modified | [InstanceEdit:391900] Matthews, L, 2009-02-25 04:39:37 [InstanceEdit:392795] Matthews, L, 2009-03-08 07:11:56 |
| text | 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. |
| (summation) | [Reaction:389954] Hydrolysis of ATP and release of tubulin folding intermediate from CCT/TriC [Homo sapiens] [Reaction:391408] Hydrolysis of ATP and release of tubulin folding intermediate from CCT/TriC [Mus musculus] |
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No pathways have been reviewed or authored by Group II chaperonins enclose substrate proteins following su... (391885)
