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7Y7H

Structure of the Bacterial Ribosome with human tRNA Tyr(GalQ34) and mRNA(UAC)

This is a non-PDB format compatible entry.
Summary for 7Y7H
Entry DOI10.2210/pdb7y7h/pdb
EMDB information33665
Descriptor16S rRNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (57 entities in total)
Functional Keywordsribosome, trna modifications, decoding
Biological sourceEscherichia coli
More
Total number of polymer chains55
Total formula weight2208155.76
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 citationZhao, 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: 37992713
DOI: 10.1016/j.cell.2023.10.026
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.51 Å)
Structure validation

227561

數據於2024-11-20公開中

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