5GAK

Yeast 60S ribosomal subunit with A-site tRNA, P-site tRNA and eIF-5A

This is a non-PDB format compatible entry.

Summary for 5GAK

• Entry DOI: 10.2210/pdb5gak/pdb
• EMDB information: 3227
• Descriptor: 25S rRNA, 60S ribosomal protein L27-A, 60S ribosomal protein L42-A, ... (50 entities in total)
• Functional Keywords: ribosome, translation, hypusine
• Biological source: Saccharomyces cerevisiae (Baker's yeast); More
• Total number of polymer chains: 49
• Total formula weight: 2016966.03

Authors

Schmidt, C.,Becker, T. (deposition date: 2015-12-09, release date: 2016-02-24, Last modification date: 2024-10-23)

Primary citation

Schmidt, C.,Becker, T.,Heuer, A.,Braunger, K.,Shanmuganathan, V.,Pech, M.,Berninghausen, O.,Wilson, D.N.,Beckmann, R.
Structure of the hypusinylated eukaryotic translation factor eIF-5A bound to the ribosome.
Nucleic Acids Res., 44:1944-1951, 2016

PubMed Abstract: During protein synthesis, ribosomes become stalled on polyproline-containing sequences, unless they are rescued in archaea and eukaryotes by the initiation factor 5A (a/eIF-5A) and in bacteria by the homologous protein EF-P. While a structure of EF-P bound to the 70S ribosome exists, structural insight into eIF-5A on the 80S ribosome has been lacking. Here we present a cryo-electron microscopy reconstruction of eIF-5A bound to the yeast 80S ribosome at 3.9 Å resolution. The structure reveals that the unique and functionally essential post-translational hypusine modification reaches toward the peptidyltransferase center of the ribosome, where the hypusine moiety contacts A76 of the CCA-end of the P-site tRNA. These findings would support a model whereby eIF-5A stimulates peptide bond formation on polyproline-stalled ribosomes by stabilizing and orienting the CCA-end of the P-tRNA, rather than by directly contributing to the catalysis.

PubMed: 26715760
DOI: 10.1093/nar/gkv1517

Experimental method

ELECTRON MICROSCOPY (3.88 Å)