8P2K

Ternary complex of translating ribosome, NAC and METAP1

This is a non-PDB format compatible entry.

Summary for 8P2K

• Entry DOI: 10.2210/pdb8p2k/pdb
• EMDB information: 17367
• Descriptor: 28S rRNA, 60S ribosomal protein L7a, 60S ribosomal protein L9, ... (97 entities in total)
• Functional Keywords: ribosome, methionine aminopeptidase 1, methionine excision, protein biogenesis, nascent chain, translation
• Biological source: Oryctolagus cuniculus (rabbit); More
• Total number of polymer chains: 88
• Total formula weight: 3984430.61

Authors

Jia, M.,Jaskolowski, M.,Scaiola, A.,Jomaa, A.,Ban, N. (deposition date: 2023-05-16, release date: 2023-07-19, Last modification date: 2024-04-24)

Primary citation

Gamerdinger, M.,Jia, M.,Schloemer, R.,Rabl, L.,Jaskolowski, M.,Khakzar, K.M.,Ulusoy, Z.,Wallisch, A.,Jomaa, A.,Hunaeus, G.,Scaiola, A.,Diederichs, K.,Ban, N.,Deuerling, E.
NAC controls cotranslational N-terminal methionine excision in eukaryotes.
Science, 380:1238-1243, 2023

PubMed Abstract: N-terminal methionine excision from newly synthesized proteins, catalyzed cotranslationally by methionine aminopeptidases (METAPs), is an essential and universally conserved process that plays a key role in cell homeostasis and protein biogenesis. However, how METAPs interact with ribosomes and how their cleavage specificity is ensured is unknown. We discovered that in eukaryotes the nascent polypeptide-associated complex (NAC) controls ribosome binding of METAP1. NAC recruits METAP1 using a long, flexible tail and provides a platform for the formation of an active methionine excision complex at the ribosomal tunnel exit. This mode of interaction ensures the efficient excision of methionine from cytosolic proteins, whereas proteins targeted to the endoplasmic reticulum are spared. Our results suggest a broader mechanism for how access of protein biogenesis factors to translating ribosomes is controlled.

PubMed: 37347872
DOI: 10.1126/science.adg3297

Experimental method

ELECTRON MICROSCOPY (2.9 Å)