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@ARTICLE{Cong:111906,
      author       = {Cong, Y and Schröder, G.F. and Meyer, A.S. and Jakana, J.
                      and Ma, B. and Dougherty, M.T. and Schmid, M.F. and
                      Reissmann, S. and Levitt, M. and Ludtke, S.L. and Frydman,
                      J. and Chiu, W.},
      title        = {{S}ymmetry-{F}ree {C}ryo-{EM} {S}tructures of the
                      {C}haperonin {TR}i{C} {A}long its {ATP}ase-{D}riven
                      {C}onformational {C}ycle},
      journal      = {The EMBO journal online},
      volume       = {31},
      issn         = {0261-4189},
      address      = {London [u.a.]},
      publisher    = {Nature Publishing Group},
      reportid     = {PreJuSER-111906},
      pages        = {720 - 730},
      year         = {2011},
      note         = {Record converted from VDB: 16.11.2012},
      abstract     = {The eukaryotic group II chaperonin TRiC/CCT is a 16-subunit
                      complex with eight distinct but similar subunits arranged in
                      two stacked rings. Substrate folding inside the central
                      chamber is triggered by ATP hydrolysis. We present five
                      cryo-EM structures of TRiC in apo and nucleotide-induced
                      states without imposing symmetry during the 3D
                      reconstruction. These structures reveal the intra- and
                      inter-ring subunit interaction pattern changes during the
                      ATPase cycle. In the apo state, the subunit arrangement in
                      each ring is highly asymmetric, whereas all
                      nucleotide-containing states tend to be more symmetrical. We
                      identify and structurally characterize an one-ring closed
                      intermediate induced by ATP hydrolysis wherein the closed
                      TRiC ring exhibits an observable chamber expansion. This
                      likely represents the physiological substrate folding state.
                      Our structural results suggest mechanisms for
                      inter-ring-negative cooperativity, intra-ring-positive
                      cooperativity, and protein-folding chamber closure of TRiC.
                      Intriguingly, these mechanisms are different from other
                      group I and II chaperonins despite their similar
                      architecture.},
      keywords     = {Adenosine Triphosphatases: metabolism / Chaperonins:
                      chemistry / Chaperonins: metabolism / Cryoelectron
                      Microscopy / Hydrolysis / Models, Molecular / Protein
                      Conformation / Protein Folding / Adenosine Triphosphatases
                      (NLM Chemicals) / Chaperonins (NLM Chemicals)},
      cin          = {ICS-6},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {Funktion und Dysfunktion des Nervensystems / BioSoft:
                      Makromolekulare Systeme und biologische
                      Informationsverarbeitung},
      pid          = {G:(DE-Juel1)FUEK409 / G:(DE-Juel1)FUEK505},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:22045336},
      pmc          = {pmc:PMC3273382},
      UT           = {WOS:000300871700019},
      doi          = {10.1038/emboj.2011.366},
      url          = {https://juser.fz-juelich.de/record/111906},
}