The 2.9 Å Crystal Structure of <i>T. thermophilus</i> Seryl-tRNA Synthetase Complexed with tRNA <sup> <i>Ser</i> </sup>

DOI Web Site 被引用文献17件
  • Valérie Biou
    European Molecular Biology Laboratory, Grenoble Outstation, 156X, 38042 Grenoble Cedex, France.
  • Anna Yaremchuk
    European Molecular Biology Laboratory, Grenoble Outstation, 156X, 38042 Grenoble Cedex, France.
  • Michael Tukalo
    European Molecular Biology Laboratory, Grenoble Outstation, 156X, 38042 Grenoble Cedex, France.
  • Stephen Cusack
    European Molecular Biology Laboratory, Grenoble Outstation, 156X, 38042 Grenoble Cedex, France.

抄録

<jats:p> The crystal structure of <jats:italic>Thermus thermophilus</jats:italic> seryl-transfer RNA synthetase, a class 2 aminoacyl-tRNA synthetase, complexed with a single tRNA <jats:sup>Ser</jats:sup> molecule was solved at 2.9 Å resolution. The structure revealed how insertion of conserved base G20b from the D loop into the core of the tRNA determines the orientation of the long variable arm, which is a characteristic feature of most serine specific tRNAs. On tRNA binding, the antiparallel coiled-coil domain of one subunit of the synthetase makes contacts with the variable arm and TψC loop of the tRNA and directs the acceptor stem of the tRNA into the active site of the other subunit. Specificity depends principally on recognition of the shape of tRNA <jats:sup>Ser</jats:sup> through backbone contacts and secondarily on sequence specific interactions. </jats:p>

収録刊行物

  • Science

    Science 263 (5152), 1404-1410, 1994-03-11

    American Association for the Advancement of Science (AAAS)

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