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Title | Dual action of ATP hydrolysis couples lid closure to substrate release into the group II chaperonin chamber. |
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Journal, issue, pages | Cell, Vol. 144, Issue 2, Page 240-252, Year 2011 |
Publish date | Jan 21, 2011 |
Authors | Nicholai R Douglas / Stefanie Reissmann / Junjie Zhang / Bo Chen / Joanita Jakana / Ramya Kumar / Wah Chiu / Judith Frydman / |
PubMed Abstract | Group II chaperonins are ATP-dependent ring-shaped complexes that bind nonnative polypeptides and facilitate protein folding in archaea and eukaryotes. A built-in lid encapsulates substrate proteins ...Group II chaperonins are ATP-dependent ring-shaped complexes that bind nonnative polypeptides and facilitate protein folding in archaea and eukaryotes. A built-in lid encapsulates substrate proteins within the central chaperonin chamber. Here, we describe the fate of the substrate during the nucleotide cycle of group II chaperonins. The chaperonin substrate-binding sites are exposed, and the lid is open in both the ATP-free and ATP-bound prehydrolysis states. ATP hydrolysis has a dual function in the folding cycle, triggering both lid closure and substrate release into the central chamber. Notably, substrate release can occur in the absence of a lid, and lid closure can occur without substrate release. However, productive folding requires both events, so that the polypeptide is released into the confined space of the closed chamber where it folds. Our results show that ATP hydrolysis coordinates the structural and functional determinants that trigger productive folding. |
External links | Cell / PubMed:21241893 / PubMed Central |
Methods | EM (single particle) |
Resolution | 4.9 - 11.0 Å |
Structure data | EMDB-5248, PDB-3izl: |
Source |
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Keywords | CHAPERONE / Mm-cpn / maripaludis / chaperonin |