Cryo-EM structure and rRNA model of a translating eukaryotic 80S ribosome at 
5.5-angstrom resolution.

Armache, J. P.; Jarasch, A.; Anger, A. M.; Villa, E.; Becker, T.; Bhushan, S.; Jossinet, F.; Habeck, M.; Dindar, G.; Franckenberg, S.; Marquez, V.; Mielke, T.; Thomm, M.; Berninghausen, O.; Beatrix, B.; Söding, J.; Westhof, E.; Wilson, D. N.; Beckmann, R.

doi:10.1073/pnas.1009999107

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Cryo-EM structure and rRNA model of a translating eukaryotic 80S ribosome at 5.5-angstrom resolution.

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Söding, J.
Research Group of Computational Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Citation

Armache, J. P., Jarasch, A., Anger, A. M., Villa, E., Becker, T., Bhushan, S., et al. (2010). Cryo-EM structure and rRNA model of a translating eukaryotic 80S ribosome at 5.5-angstrom resolution. Proceedings of the National Academy of Sciences of the United States of America, 107(46), 19748-19753. doi:10.1073/pnas.1009999107.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0017-93AB-6

Abstract

Protein biosynthesis, the translation of the genetic code into polypeptides, occurs on ribonucleoprotein particles called ribosomes. Although X-ray structures of bacterial ribosomes are available, high-resolution structures of eukaryotic 80S ribosomes are lacking. Using cryoelectron microscopy and single-particle reconstruction, we have determined the structure of a translating plant (Triticum aestivum) 80S ribosome at 5.5-Å resolution. This map, together with a 6.1-Å map of a Saccharomyces cerevisiae 80S ribosome, has enabled us to model ∼98% of the rRNA. Accurate assignment of the rRNA expansion segments (ES) and variable regions has revealed unique ES–ES and r-protein–ES interactions, providing insight into the structure and evolution of the eukaryotic ribosome.