Visualizing GroEL/ES in the Act of Encapsulating a Folding Protein

@article{Chen2013VisualizingGI,
  title={Visualizing GroEL/ES in the Act of Encapsulating a Folding Protein},
  author={D Chen and Damian Madan and Jeremy Weaver and Zong X. Lin and Gunnar F. Schr{\"o}der and Wah Chiu and Hays S. Rye},
  journal={Cell},
  year={2013},
  volume={153},
  pages={1354-1365}
}
The GroEL/ES chaperonin system is required for the assisted folding of many proteins. How these substrate proteins are encapsulated within the GroEL-GroES cavity is poorly understood. Using symmetry-free, single-particle cryo-electron microscopy, we have characterized a chemically modified mutant of GroEL (EL43Py) that is trapped at a normally transient stage of substrate protein encapsulation. We show that the symmetric pattern of the GroEL subunits is broken as the GroEL cis-ring apical… CONTINUE READING
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