SNAP annotations: PDB entry 7bhp

PDB-id

7bhp; DSSR-derived features in text and JSON formats; DNAproDB

Class

ribosome

Method

cryo-EM (3.3 Å)

Summary

cryo-EM structure of the human ebp1 - 80s ribosome

Reference

Bhaskar V, Desogus J, Graff-Meyer A, Schenk AD, Cavadini S, Chao JA (2021): "Dynamic association of human Ebp1 with the ribosome." Rna, 27, 411-419. doi: 10.1261/rna.077602.120.

Abstract

Ribosomes are the macromolecular machines at the heart of protein synthesis; however, their function can be modulated by a variety of additional protein factors that directly interact with them. Here, we report the cryo-EM structure of human Ebp1 (p48 isoform) bound to the human 80S ribosome at 3.3 Å resolution. Ebp1 binds in the vicinity of the peptide exit tunnel on the 80S ribosome, and this binding is enhanced upon puromycin-mediated translational inhibition. The association of Ebp1 with the 80S ribosome centers around its interaction with ribosomal proteins eL19 and uL23 and the 28S rRNA. Further analysis of the Ebp1-ribosome complex suggests that Ebp1 can rotate around its insert domain, which may enable it to assume a wide range of conformations while maintaining its interaction with the ribosome. Structurally, Ebp1 shares homology with the methionine aminopeptidase 2 family of enzymes; therefore, this inherent flexibility may also be conserved.