9GJ5
Human 80S ribosome in complex with NatA in distal position and Ebp1
This is a non-PDB format compatible entry.
Summary for 9GJ5
| Entry DOI | 10.2210/pdb9gj5/pdb |
| EMDB information | 51382 |
| Descriptor | N-alpha-acetyltransferase 10, 60S ribosomal protein L23a, 60S ribosomal protein L19, ... (14 entities in total) |
| Functional Keywords | human 80s ribosome, n-terminal acetylation (nta), n-acety-transferase a (nata), ebp1, pa2g4, translation |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 13 |
| Total formula weight | 2031396.75 |
| 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 Cited by 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: 41577663DOI: 10.1038/s41467-026-68787-5 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.61 Å) |
Structure validation
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