7bhp

Publication Abstract from PubMed

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 A 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.

Dynamic association of human Ebp1 with the ribosome.,Bhaskar V, Desogus J, Graff-Meyer A, Schenk AD, Cavadini S, Chao JA RNA. 2021 Apr;27(4):411-419. doi: 10.1261/rna.077602.120. Epub 2021 Jan 21. PMID:33479117^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.