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@ARTICLE{Chen:139201,
      author       = {Chen, D. -H. and Madan, D. and Weaver, J. and Lin, Z. and
                      Schröder, Gunnar F. and Chiu, W. and Rye, H. S.},
      title        = {{V}isualizing {G}ro{EL}/{ES} in the {A}ct of
                      {E}ncapsulating a {F}olding {P}rotein},
      journal      = {Cell},
      volume       = {153},
      number       = {6},
      issn         = {1097-4172},
      address      = {[Cambridge, Mass.]},
      publisher    = {Cell Press},
      reportid     = {FZJ-2013-05204},
      pages        = {1354-1365},
      year         = {2013},
      abstract     = {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 domains reorient to
                      accommodate the simultaneous binding of GroES and an
                      incompletely folded substrate protein (RuBisCO). The
                      collapsed RuBisCO folding intermediate binds to the lower
                      segment of two apical domains, as well as to the normally
                      unstructured GroEL C-terminal tails. A comparative
                      structural analysis suggests that the allosteric transitions
                      leading to substrate protein release and folding involve
                      concerted shifts of GroES and the GroEL apical domains and
                      C-terminal tails.},
      cin          = {ICS-6},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {452 - Structural Biology (POF2-452)},
      pid          = {G:(DE-HGF)POF2-452},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000319979200018},
      pubmed       = {pmid:23746846},
      doi          = {10.1016/j.cell.2013.04.052},
      url          = {https://juser.fz-juelich.de/record/139201},
}