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@ARTICLE{Zhang:8698,
      author       = {Zhang, J. and Baker, M.L. and Schröder, G.F. and Douglas,
                      N.R. and Reissmann, S. and Jakana, J. and Dougherty, M. and
                      Fu, C.J. and Levitt, M. and Ludtke, S.J. and Frydman, J. and
                      Chiu, W.},
      title        = {{M}echanism of folding chamber closure in a group {II}
                      chaperonin},
      journal      = {Nature},
      volume       = {463},
      issn         = {0028-0836},
      address      = {London [u.a.]},
      publisher    = {Nature Publising Group},
      reportid     = {PreJuSER-8698},
      pages        = {379 - 383},
      year         = {2010},
      note         = {We acknowledge the support of grants from the National
                      Institutes of Health through the Nanomedicine Development
                      Center Roadmap Initiative, Biomedical Technology Research
                      Center for Structural Biology in National Center for
                      Research Resources, Nanobiology Training Fellowship
                      administered by the Keck Center of the Gulf Coast Consortia
                      and the National Science Foundation.},
      abstract     = {Group II chaperonins are essential mediators of cellular
                      protein folding in eukaryotes and archaea. These oligomeric
                      protein machines, approximately 1 megadalton, consist of two
                      back-to-back rings encompassing a central cavity that
                      accommodates polypeptide substrates. Chaperonin-mediated
                      protein folding is critically dependent on the closure of a
                      built-in lid, which is triggered by ATP hydrolysis. The
                      structural rearrangements and molecular events leading to
                      lid closure are still unknown. Here we report four single
                      particle cryo-electron microscopy (cryo-EM) structures of
                      Mm-cpn, an archaeal group II chaperonin, in the
                      nucleotide-free (open) and nucleotide-induced (closed)
                      states. The 4.3 A resolution of the closed conformation
                      allowed building of the first ever atomic model directly
                      from the single particle cryo-EM density map, in which we
                      were able to visualize the nucleotide and more than $70\%$
                      of the side chains. The model of the open conformation was
                      obtained by using the deformable elastic network modelling
                      with the 8 A resolution open-state cryo-EM density
                      restraints. Together, the open and closed structures show
                      how local conformational changes triggered by ATP hydrolysis
                      lead to an alteration of intersubunit contacts within and
                      across the rings, ultimately causing a rocking motion that
                      closes the ring. Our analyses show that there is an
                      intricate and unforeseen set of interactions controlling
                      allosteric communication and inter-ring signalling, driving
                      the conformational cycle of group II chaperonins. Beyond
                      this, we anticipate that our methodology of combining single
                      particle cryo-EM and computational modelling will become a
                      powerful tool in the determination of atomic details
                      involved in the dynamic processes of macromolecular machines
                      in solution.},
      keywords     = {Adenosine Triphosphate: chemistry / Adenosine Triphosphate:
                      metabolism / Adenosine Triphosphate: pharmacology /
                      Allosteric Regulation / Binding Sites / Cryoelectron
                      Microscopy / Group II Chaperonins: chemistry / Group II
                      Chaperonins: metabolism / Group II Chaperonins:
                      ultrastructure / Hydrolysis: drug effects / Methanococcus:
                      chemistry / Models, Molecular / Protein Binding / Protein
                      Conformation: drug effects / Protein Folding / Protein
                      Subunits: chemistry / Protein Subunits: metabolism /
                      Structure-Activity Relationship / Protein Subunits (NLM
                      Chemicals) / Adenosine Triphosphate (NLM Chemicals) / Group
                      II Chaperonins (NLM Chemicals) / J (WoSType)},
      cin          = {ISB-3},
      ddc          = {070},
      cid          = {I:(DE-Juel1)VDB942},
      pnm          = {Funktion und Dysfunktion des Nervensystems / BioSoft:
                      Makromolekulare Systeme und biologische
                      Informationsverarbeitung},
      pid          = {G:(DE-Juel1)FUEK409 / G:(DE-Juel1)FUEK505},
      shelfmark    = {Multidisciplinary Sciences},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:20090755},
      pmc          = {pmc:PMC2834796},
      UT           = {WOS:000273748100049},
      doi          = {10.1038/nature08701},
      url          = {https://juser.fz-juelich.de/record/8698},
}