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Title | Cryo-EM structure and rRNA model of a translating eukaryotic 80S ribosome at 5.5-A resolution. |
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Journal, issue, pages | Proc Natl Acad Sci U S A, Vol. 107, Issue 46, Page 19748-19753, Year 2010 |
Publish date | Nov 16, 2010 |
Authors | Jean-Paul Armache / Alexander Jarasch / Andreas M Anger / Elizabeth Villa / Thomas Becker / Shashi Bhushan / Fabrice Jossinet / Michael Habeck / Gülcin Dindar / Sibylle Franckenberg / Viter Marquez / Thorsten Mielke / Michael Thomm / Otto Berninghausen / Birgitta Beatrix / Johannes Söding / Eric Westhof / Daniel N Wilson / Roland Beckmann / |
PubMed 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, ...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. |
External links | Proc Natl Acad Sci U S A / PubMed:20980660 / PubMed Central |
Methods | EM (single particle) |
Resolution | 8.6 - 8.8 Å |
Structure data | PDB-3izd: PDB-4v6i: |
Source |
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Keywords | RIBOSOME / eukaryotic ribosome / homology modelling / de novo modeling / ribosomal RNA / rRNA / RNA expansion segments / homology modeling / ribosomal proteins / novel ribosomal proteins |