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

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, Gregers R. Andersen () and Roland Beckmann ()
Additional contact information
Christian B. F. Andersen: University of Aarhus
Thomas Becker: Institute of Biochemistry, Charité, University Medical School, Humboldt University of Berlin
Michael Blau: Institute of Biochemistry, Charité, University Medical School, Humboldt University of Berlin
Monika Anand: UMDNJ Robert Wood Johnson Medical School
Mario Halic: Institute of Biochemistry, Charité, University Medical School, Humboldt University of Berlin
Bharvi Balar: 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
Gregers R. Andersen: University of Aarhus
Roland Beckmann: Institute of Biochemistry, Charité, University Medical School, Humboldt University of Berlin

Nature, 2006, vol. 443, issue 7112, 663-668

Abstract: 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.

Date: 2006
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DOI: 10.1038/nature05126

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