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Title | Structure of the hypusinylated eukaryotic translation factor eIF-5A bound to the ribosome. |
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Journal, issue, pages | Nucleic Acids Res, Vol. 44, Issue 4, Page 1944-1951, Year 2016 |
Publish date | Feb 29, 2016 |
Authors | Christian Schmidt / Thomas Becker / André Heuer / Katharina Braunger / Vivekanandan Shanmuganathan / Markus Pech / Otto Berninghausen / Daniel N Wilson / Roland Beckmann / |
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 ...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. |
External links | Nucleic Acids Res / PubMed:26715760 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.88 Å |
Structure data | |
Chemicals | ChemComp-3HE: |
Source |
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Keywords | RIBOSOME / translation / hypusine |