9F1D
Mammalian quaternary complex of a translating 80S ribosome, NAC, MetAP1 and NatA/E-HYPK
This is a non-PDB format compatible entry.
Summary for 9F1D
| Entry DOI | 10.2210/pdb9f1d/pdb |
| Related | 2b3h 6ppl 6pw9 7qwr 8p2k |
| EMDB information | 50126 |
| Descriptor | 28S rRNA, 5.8S rRNA, 60S ribosomal protein L22, ... (99 entities in total) |
| Functional Keywords | translation, ribosome, nac, n-terminal acetyltransferase, nata, nate, metap1, hypk |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 91 |
| Total formula weight | 4125657.36 |
| Authors | Yudin, D.,Scaiola, A.,Ban, N. (deposition date: 2024-04-18, release date: 2024-08-21, Last modification date: 2024-10-02) |
| Primary citation | Lentzsch, A.M.,Yudin, D.,Gamerdinger, M.,Chandrasekar, S.,Rabl, L.,Scaiola, A.,Deuerling, E.,Ban, N.,Shan, S.O. NAC guides a ribosomal multienzyme complex for nascent protein processing. Nature, 633:718-724, 2024 Cited by PubMed Abstract: Approximately 40% of the mammalian proteome undergoes N-terminal methionine excision and acetylation, mediated sequentially by methionine aminopeptidase (MetAP) and N-acetyltransferase A (NatA), respectively. Both modifications are strictly cotranslational and essential in higher eukaryotic organisms. The interaction, activity and regulation of these enzymes on translating ribosomes are poorly understood. Here we perform biochemical, structural and in vivo studies to demonstrate that the nascent polypeptide-associated complex (NAC) orchestrates the action of these enzymes. NAC assembles a multienzyme complex with MetAP1 and NatA early during translation and pre-positions the active sites of both enzymes for timely sequential processing of the nascent protein. NAC further releases the inhibitory interactions from the NatA regulatory protein huntingtin yeast two-hybrid protein K (HYPK) to activate NatA on the ribosome, enforcing cotranslational N-terminal acetylation. Our results provide a mechanistic model for the cotranslational processing of proteins in eukaryotic cells. PubMed: 39169182DOI: 10.1038/s41586-024-07846-7 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.26 Å) |
Structure validation
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