EMD-3227

Single-particle
3.88 Å
EMD-3227 Deposition: 29/10/2015
Map released: 13/01/2016
Last modified: 16/03/2016
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-3227

Cryo-EM map of a native 80S-ribosome-eIF-5A complex

EMD-3227

Single-particle
3.88 Å
EMD-3227 Deposition: 29/10/2015
Map released: 13/01/2016
Last modified: 16/03/2016
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Saccharomyces cerevisiae
Sample: Native 80S ribosome-eIF-5A complex from yeast
Fitted models: 5gak (Avg. Q-score: -0.012)

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