GroEL/GroES: structure and function of a two-stroke folding machine.

@article{Xu1998GroELGroESSA,
  title={GroEL/GroES: structure and function of a two-stroke folding machine.},
  author={Zhigang Xu and Paul B. Sigler},
  journal={Journal of structural biology},
  year={1998},
  volume={124 2-3},
  pages={129-41}
}
Recent structural and functional studies have greatly advanced our understanding of the mechanism by which chaperonins (Cpn60) mediate protein folding, the final step in the accurate expression of genetic information. Escherichia coli GroEL has a symmetric double-toroid architecture, which binds nonnative polypeptide substrates on the hydrophobic walls of its central cavity. The asymmetric binding of ATP and cochaperonin GroES to GroEL triggers a major conformational change in the cis ring… CONTINUE READING
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