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TitleDynamic association of human Ebp1 with the ribosome.
Journal, issue, pagesRNA, Vol. 27, Issue 4, Page 411-419, Year 2021
Publish dateJan 21, 2021
AuthorsVarun Bhaskar / Jessica Desogus / Alexandra Graff-Meyer / Andreas D Schenk / Simone Cavadini / Jeffrey A Chao /
PubMed AbstractRibosomes 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. ...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.
External linksRNA / PubMed:33479117 / PubMed Central
MethodsEM (single particle)
Resolution3.3 Å
Structure data

12189

7bhp

EMDB-12189, PDB-7bhp:
Cryo-EM structure of the human Ebp1 - 80S ribosome
Method: EM (single particle) / Resolution: 3.3 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
  • Human (human)
KeywordsRIBOSOME / EBP1 / PAG2G4 / MetAP2 / metalloprotease / ES27 / ribosomal tunnel exit

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