Essential function of the built-in lid in the allosteric regulation of eukaryotic and archaeal chaperonins

@article{Reissmann2007EssentialFO,
  title={Essential function of the built-in lid in the allosteric regulation of eukaryotic and archaeal chaperonins},
  author={Stefanie Reissmann and Charles Parnot and Christopher R. Booth and Wah Chiu and Judith Frydman},
  journal={Nature Structural &Molecular Biology},
  year={2007},
  volume={14},
  pages={432-440}
}
Chaperonins are allosteric double-ring ATPases that mediate cellular protein folding. ATP binding and hydrolysis control opening and closing of the central chaperonin chamber, which transiently provides a protected environment for protein folding. During evolution, two strategies to close the chaperonin chamber have emerged. Archaeal and eukaryotic group II chaperonins contain a built-in lid, whereas bacterial chaperonins use a ring-shaped cofactor as a detachable lid. Here we show that the… CONTINUE READING
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