9RUA
RPS26dC HEK mutant 80S ribosome bound to TISU mRNA (RPS26dC-TISU)
This is a non-PDB format compatible entry.
Summary for 9RUA
| Entry DOI | 10.2210/pdb9rua/pdb |
| EMDB information | 54268 |
| Descriptor | Ubiquitin-60S ribosomal protein L40, 40S ribosomal protein S16, 40S ribosomal protein S14, ... (86 entities in total) |
| Functional Keywords | 80s ribosome, tisu mrna, human, es26, rps26dc, ribosome |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 80 |
| Total formula weight | 3816520.11 |
| Authors | Hiregange, D.G.,Fraticelli, D.,Bashan, A.,Yonath, A.,Dikstein, R. (deposition date: 2025-07-03, release date: 2026-06-03) |
| Primary citation | Fraticelli, D.,Hiregange, D.G.,Weiss, B.,Ogran, A.,Havkin-Solomon, T.,Roman, I.M.,Bashan, A.,Yonath, A.,Dikstein, R. Structural and molecular basis of specialized translation mediated by the ribosome mRNA-binding channel. Nat Commun, 2026 Cited by PubMed Abstract: The ribosome mRNA channel is central to translation, yet its role in regulatory mechanisms remains unclear. Using cryo-EM of human ribosomal complexes bound to Kozak and TISU mRNAs from wild-type (WT) and RPS26/eS26 mutant (RPS26dC) cells, we demonstrate that both RPS26/eS26 and mRNA adopt distinct conformations, explaining the opposing effects of RPS26dC on their activity. Translatome studies of WT and RPS26dC reveal AUG-context-dependent changes in 48S and 80S initiation complexes and slower scanning. Downregulated mRNAs are enriched for specific AUG-upstream nucleotides and a -1-cytosine contacting 18S rRNA G1207, an interaction lost in RPS26dC. Strongly affected transcripts include replication-dependent histones, which, despite short 5'UTRs and suboptimal Kozak, exhibit robust translation activity that is RPS26/eS26-dependent. We identify a translational enhancer in the H2B 5'UTR (-16 to -9) overlapping predicted RPS26/eS26-binding sites, with a distinct ribosome-bound conformation. Exploiting these features, we engineered a high-efficiency translational cassette with minimal leaky scanning. These findings underscore the role of the ribosome's mRNA channel in selective translation and its therapeutic potential. PubMed: 42056121DOI: 10.1038/s41467-026-72263-5 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.9 Å) |
Structure validation
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