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Structure of eEF3 and the mechanism of transfer RNA release from the E-site

Author

Listed:
  • Christian B. F. Andersen

    (University of Aarhus)

  • Thomas Becker

    (Institute of Biochemistry, Charité, University Medical School, Humboldt University of Berlin
    University of Munich)

  • Michael Blau

    (Institute of Biochemistry, Charité, University Medical School, Humboldt University of Berlin)

  • Monika Anand

    (UMDNJ Robert Wood Johnson Medical School
    Immunology, UMDNJ Robert Wood Johnson Medical School)

  • Mario Halic

    (Institute of Biochemistry, Charité, University Medical School, Humboldt University of Berlin
    University of Munich)

  • Bharvi Balar

    (UMDNJ Robert Wood Johnson Medical School
    Immunology, UMDNJ Robert Wood Johnson Medical School)

  • Thorsten Mielke

    (UltraStructureNetwork, USN, Max Planck Institute for Molecular Genetics)

  • Thomas Boesen

    (University of Aarhus)

  • Jan Skov Pedersen

    (University of Aarhus)

  • Christian M. T. Spahn

    (Institut für Medizinische Physik und Biophysik, Charité, University Medical School, Humboldt University of Berlin)

  • Terri Goss Kinzy

    (UMDNJ Robert Wood Johnson Medical School
    Immunology, UMDNJ Robert Wood Johnson Medical School)

  • Gregers R. Andersen

    (University of Aarhus)

  • Roland Beckmann

    (Institute of Biochemistry, Charité, University Medical School, Humboldt University of Berlin
    University of Munich)

Abstract

Elongation factor eEF3 is an ATPase that, in addition to the two canonical factors eEF1A and eEF2, serves an essential function in the translation cycle of fungi. eEF3 is required for the binding of the aminoacyl-tRNA–eEF1A–GTP ternary complex to the ribosomal A-site and has been suggested to facilitate the clearance of deacyl-tRNA from the E-site. Here we present the crystal structure of Saccharomyces cerevisiae eEF3, showing that it consists of an amino-terminal HEAT repeat domain, followed by a four-helix bundle and two ABC-type ATPase domains, with a chromodomain inserted in ABC2. Moreover, we present the cryo-electron microscopy structure of the ATP-bound form of eEF3 in complex with the post-translocational-state 80S ribosome from yeast. eEF3 uses an entirely new factor binding site near the ribosomal E-site, with the chromodomain likely to stabilize the ribosomal L1 stalk in an open conformation, thus allowing tRNA release.

Suggested Citation

  • Christian B. F. Andersen & Thomas Becker & Michael Blau & Monika Anand & Mario Halic & Bharvi Balar & Thorsten Mielke & Thomas Boesen & Jan Skov Pedersen & Christian M. T. Spahn & Terri Goss Kinzy & G, 2006. "Structure of eEF3 and the mechanism of transfer RNA release from the E-site," Nature, Nature, vol. 443(7112), pages 663-668, October.
    • Handle: RePEc:nat:nature:v:443:y:2006:i:7112:d:10.1038_nature05126
    DOI: 10.1038/nature05126
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