7Y7C
Structure of the Bacterial Ribosome with human tRNA Asp(G34) and mRNA(GAU)
This is a non-PDB format compatible entry.
Summary for 7Y7C
| Entry DOI | 10.2210/pdb7y7c/pdb |
| EMDB information | 33660 |
| Descriptor | 16S rRNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (56 entities in total) |
| Functional Keywords | trna modifications, decoding, ribosome |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 55 |
| Total formula weight | 2207859.11 |
| Authors | Ishiguro, K.,Yokoyama, T.,Shirouzu, M.,Suzuki, T. (deposition date: 2022-06-22, release date: 2023-10-25, Last modification date: 2023-12-27) |
| Primary citation | Zhao, X.,Ma, D.,Ishiguro, K.,Saito, H.,Akichika, S.,Matsuzawa, I.,Mito, M.,Irie, T.,Ishibashi, K.,Wakabayashi, K.,Sakaguchi, Y.,Yokoyama, T.,Mishima, Y.,Shirouzu, M.,Iwasaki, S.,Suzuki, T.,Suzuki, T. Glycosylated queuosines in tRNAs optimize translational rate and post-embryonic growth. Cell, 186:5517-, 2023 Cited by PubMed Abstract: Transfer RNA (tRNA) modifications are critical for protein synthesis. Queuosine (Q), a 7-deaza-guanosine derivative, is present in tRNA anticodons. In vertebrate tRNAs for Tyr and Asp, Q is further glycosylated with galactose and mannose to generate galQ and manQ, respectively. However, biogenesis and physiological relevance of Q-glycosylation remain poorly understood. Here, we biochemically identified two RNA glycosylases, QTGAL and QTMAN, and successfully reconstituted Q-glycosylation of tRNAs using nucleotide diphosphate sugars. Ribosome profiling of knockout cells revealed that Q-glycosylation slowed down elongation at cognate codons, UAC and GAC (GAU), respectively. We also found that galactosylation of Q suppresses stop codon readthrough. Moreover, protein aggregates increased in cells lacking Q-glycosylation, indicating that Q-glycosylation contributes to proteostasis. Cryo-EM of human ribosome-tRNA complex revealed the molecular basis of codon recognition regulated by Q-glycosylations. Furthermore, zebrafish qtgal and qtman knockout lines displayed shortened body length, implying that Q-glycosylation is required for post-embryonic growth in vertebrates. PubMed: 37992713DOI: 10.1016/j.cell.2023.10.026 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.51 Å) |
Structure validation
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