9GJ6

Human 80S ribosome in complex with NatA in proximal and distal position

This is a non-PDB format compatible entry.

Summary for 9GJ6

• Entry DOI: 10.2210/pdb9gj6/pdb
• EMDB information: 51383
• Descriptor: N-alpha-acetyltransferase 10, 60S ribosomal protein L23a, 60S ribosomal protein L19, ... (16 entities in total)
• Functional Keywords: human 80s ribosome, n-terminal acetylation (nta), n-acety-transferase a (nata) in proximal and distal position, translation
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 17
• Total formula weight: 2170601.99

Authors

Klein, M.A.,Wild, K.,Sinning, I. (deposition date: 2024-08-21, release date: 2026-02-18, Last modification date: 2026-06-03)

Primary citation

Klein, M.,Wild, K.,McTiernan, N.,Arnesen, T.,Sinning, I.
NatA engages in multi-factor complexes at the ribosomal polypeptide tunnel exit.
Nat Commun, 17:884-884, 2026

PubMed Abstract: N-terminal acetylation (NTA) is the most common protein modification in eukaryotes, playing a crucial role in proteostasis. Almost 40% of the human proteome is acetylated co-translationally by the NatA complex, which requires prior N-terminal methionine excision (NME). Recently, NatA was shown to form multi-enzyme complexes with MAP1/NAC or MAP2, combining the capabilities of NME and NTA into a single complex. Here, we show that NatA can also form ribosome-independent assemblies with several ribosome associated factors (RAFs). At the ribosome, NatA can form a ternary complex with the abundant pseudoenzyme Ebp1 or a second copy of NatA, which can be coordinated from a different binding site with closer access to a potential substrate. Further, we identify a conserved binding site on NatA, which can be accessed by four RAFs - Ebp1, NAC, Naa10 and HypK, allowing the formation of different multi-factor complexes at the ribosomal tunnel exit. Therefore, our data suggest that NatA constitutes an interaction hub, and contributes to the coordination of co-translational protein maturation.

PubMed: 41577663
DOI: 10.1038/s41467-026-68787-5

Experimental method

ELECTRON MICROSCOPY (3.91 Å)