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@ARTICLE{Bock:139180,
      author       = {Bock, Lars V and Blau, Christian and Schröder, Gunnar and
                      Davydov, Iakov I and Fischer, Niels and Stark, Holger and
                      Rodnina, Marina V and Vaiana, Andrea C and Grubmüller,
                      Helmut},
      title        = {{E}nergy barriers and driving forces in t{RNA}
                      translocation through the ribosome},
      journal      = {Nature structural $\&$ molecular biology},
      volume       = {2690},
      issn         = {1545-9993},
      address      = {London [u.a.]},
      publisher    = {Nature Publishing Group},
      reportid     = {FZJ-2013-05183},
      pages        = {1-8},
      year         = {2013},
      abstract     = {During protein synthesis, tRNAs move from the ribosome's
                      aminoacyl to peptidyl to exit sites. Here we investigate
                      conformational motions during spontaneous translocation,
                      using molecular dynamics simulations of 13
                      intermediate-translocation-state models obtained by
                      combining Escherichia coli ribosome crystal structures with
                      cryo-EM data. Resolving fast transitions between states, we
                      find that tRNA motions govern the transition rates within
                      the pre- and post-translocation states. Intersubunit
                      rotations and L1-stalk motion exhibit fast intrinsic
                      submicrosecond dynamics. The L1 stalk drives the tRNA from
                      the peptidyl site and links intersubunit rotation to
                      translocation. Displacement of tRNAs is controlled by
                      'sliding' and 'stepping' mechanisms involving conserved L16,
                      L5 and L1 residues, thus ensuring binding to the ribosome
                      despite large-scale tRNA movement. Our results complement
                      structural data with a time axis, intrinsic transition rates
                      and molecular forces, revealing correlated functional
                      motions inaccessible by other means.},
      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:000328007600011},
      pubmed       = {pmid:24186064},
      doi          = {10.1038/nsmb.2690},
      url          = {https://juser.fz-juelich.de/record/139180},
}