Dual Action of ATP Hydrolysis Couples Lid Closure to Substrate Release into the Group II Chaperonin Chamber

@article{Douglas2011DualAO,
  title={Dual Action of ATP Hydrolysis Couples Lid Closure to Substrate Release into the Group II Chaperonin Chamber},
  author={Nicholai R. Douglas and Stefanie Reissmann and Junjie Zhang and Bo Chen and Joanita Jakana and Ramya Kumar and Wah Chiu and Judith Frydman},
  journal={Cell},
  year={2011},
  volume={144},
  pages={240-252}
}
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… CONTINUE READING
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