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@ARTICLE{Fischer:827054,
      author       = {Fischer, Niels and Neumann, Piotr and Bock, Lars V. and
                      Maracci, Cristina and Wang, Zhe and Paleskava, Alena and
                      Konevega, Andrey L. and Schröder, Gunnar and Helmut,
                      Grubmüller and Ficner, Ralf and Rodnina, Marina V. and
                      Stark, Holger},
      title        = {{T}he pathway to {GTP}ase activation of elongation factor
                      {S}el{B} on the ribosome},
      journal      = {Nature},
      volume       = {540},
      issn         = {0028-0836},
      address      = {London [u.a.]},
      publisher    = {Nature Publ. Group},
      reportid     = {FZJ-2017-01260},
      pages        = {80–85},
      year         = {2016},
      abstract     = {In all domains of life, selenocysteine (Sec) is delivered
                      to the ribosome by selenocysteine-specific tRNA (tRNASec)
                      with the help of a specialized translation factor, SelB in
                      bacteria. Sec-tRNASec recodes a UGA stop codon next to a
                      downstream mRNA stem–loop. Here we present the structures
                      of six intermediates on the pathway of UGA recoding in
                      Escherichia coli by single-particle cryo-electron
                      microscopy. The structures explain the specificity of
                      Sec-tRNASec binding by SelB and show large-scale
                      rearrangements of Sec-tRNASec. Upon initial binding of
                      SelB–Sec-tRNASec to the ribosome and codon reading, the
                      30S subunit adopts an open conformation with Sec-tRNASec
                      covering the sarcin–ricin loop (SRL) on the 50S subunit.
                      Subsequent codon recognition results in a local closure of
                      the decoding site, which moves Sec-tRNASec away from the SRL
                      and triggers a global closure of the 30S subunit shoulder
                      domain. As a consequence, SelB docks on the SRL, activating
                      the GTPase of SelB. These results reveal how codon
                      recognition triggers GTPase activation in translational
                      GTPases.},
      cin          = {ICS-6},
      ddc          = {070},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551)},
      pid          = {G:(DE-HGF)POF3-551},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000388916600051},
      pubmed       = {pmid:27842381},
      doi          = {10.1038/nature20560},
      url          = {https://juser.fz-juelich.de/record/827054},
}