9SYR
Human quaternary complex of a translating 80S ribosome, NAC, MetAP1 and NatD
This is a non-PDB format compatible entry.
Summary for 9SYR
| Entry DOI | 10.2210/pdb9syr/pdb |
| Related | 2B3H 4U9W 6R5Q 7O7Y 7QWR 8PPK 9GMO |
| EMDB information | 55351 |
| Descriptor | 28S rRNA, 60S ribosomal protein L21, 60S ribosomal protein L22, ... (89 entities in total) |
| Functional Keywords | translation, ribosome, nac, n-terminal acetyltransferase, natd, metap1 |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 86 |
| Total formula weight | 4575498.14 |
| Authors | Yudin, D.,Jaskolowski, M.,Scaiola, A.,Ban, N. (deposition date: 2025-10-13, release date: 2025-12-17, Last modification date: 2026-01-14) |
| Primary citation | Yudin, D.,Jaskolowski, M.,Fan, Z.,Burg, N.,Chandrasekar, S.,Lentzsch, A.M.,Scaiola, A.,Bothe, A.,Deuerling, E.,Gamerdinger, M.,Shan, S.O.,Ban, N. Mechanism of cotranslational modification of histones H2A and H4 by MetAP1 and NatD. Sci Adv, 11:eaeb1017-eaeb1017, 2025 Cited by PubMed Abstract: The replication-dependent histones H2A and H4 are among the most highly expressed proteins in eukaryotes during the S phase to ensure packaging of replicated chromosomes. Nearly all newly synthesized H2A and H4 are N-terminally acetylated by N-terminal acetyltransferase D (NatD) following excision of the initiator methionine by methionine aminopeptidases (MetAPs). These modifications influence chromatin function, but how they occur cotranslationally on these exceptionally abundant and small proteins was not understood. Here, we show that the nascent polypeptide-associated complex controls the cotranslational modification of histones H2A and H4 by recruiting NatD and the upstream enzyme MetAP1 to ribosomes. MetAP1 and NatD cooperate on the ribosome to create a confined environment for the efficient sequential modification of the nascent histone chain. Our work provides a mechanistic model for the early steps of histone maturation. PubMed: 41417911DOI: 10.1126/sciadv.aeb1017 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.55 Å) |
Structure validation
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