6SXO

Cryo-EM structure of the human Ebp1-ribosome complex

This is a non-PDB format compatible entry.

Summary for 6SXO

• Entry DOI: 10.2210/pdb6sxo/pdb
• EMDB information: 10344 10608 10609
• Descriptor: Proliferation-associated protein 2G4, 60S ribosomal protein L35, 60S ribosomal protein L38, ... (8 entities in total)
• Functional Keywords: human ebp1, pa2g4 family, met-ap homolog, expansion segment es27l, ribosome
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 8
• Total formula weight: 1815935.22

Authors

Wild, K.,Aleksic, M.,Pfeffer, M.,Sinning, I. (deposition date: 2019-09-26, release date: 2020-02-19, Last modification date: 2024-05-22)

Primary citation

Wild, K.,Aleksic, M.,Lapouge, K.,Juaire, K.D.,Flemming, D.,Pfeffer, S.,Sinning, I.
MetAP-like Ebp1 occupies the human ribosomal tunnel exit and recruits flexible rRNA expansion segments.
Nat Commun, 11:776-776, 2020

PubMed Abstract: Human Ebp1 is a member of the proliferation-associated 2G4 (PA2G4) family and plays an important role in cancer regulation. Ebp1 shares the methionine aminopeptidase (MetAP) fold and binds to mature 80S ribosomes for translational control. Here, we present a cryo-EM single particle analysis reconstruction of Ebp1 bound to non-translating human 80S ribosomes at a resolution range from 3.3 to ~8 Å. Ebp1 blocks the tunnel exit with major interactions to the general uL23/uL29 docking site for nascent chain-associated factors complemented by eukaryote-specific eL19 and rRNA helix H59. H59 is defined as dynamic adaptor undergoing significant remodeling upon Ebp1 binding. Ebp1 recruits rRNA expansion segment ES27L to the tunnel exit via specific interactions with rRNA consensus sequences. The Ebp1-ribosome complex serves as a template for MetAP binding and provides insights into the structural principles for spatial coordination of co-translational events and molecular triage at the ribosomal tunnel exit.

PubMed: 32034140
DOI: 10.1038/s41467-020-14603-7

Experimental method

ELECTRON MICROSCOPY (3.3 Å)