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

MPG-Autoren
http://pubman.mpdl.mpg.de/cone/persons/resource/persons50431

Mielke,  Thorsten
Imaging/Electron Microscopy (Head: Rudi Lurz/Thorsten Mielke), Scientific Service (Head: Manuela B. Urban), Max Planck Institute for Molecular Genetics, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons50563

Spahn,  Christian M. T.
Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society;

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Volltexte (frei zugänglich)

nature05126.pdf
(beliebiger Volltext), 574KB

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Zitation

Andersen, C. B. F., Becker, T., Blau, M., Anand, M., Halic, M., Balar, B., et al. (2006). Structure of eEF3 and the mechanism of transfer RNA release from the E-site. Nature, 443(7112), 663-668. doi:10.1038/nature05126.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0010-8377-7
Zusammenfassung
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.