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8JDK

Structure of the Human cytoplasmic Ribosome with human tRNA Asp(ManQ34) and mRNA(GAU)

This is a non-PDB format compatible entry.
Summary for 8JDK
Entry DOI10.2210/pdb8jdk/pdb
Related7Y7C 7Y7D 7Y7E 7Y7F 7Y7G 7Y7H
EMDB information36179
DescriptormRNA, 60S ribosomal protein L6, 60S ribosomal protein L7, ... (82 entities in total)
Functional Keywordstrna modifications, decoding, ribosome
Biological sourceHomo sapiens
More
Total number of polymer chains80
Total formula weight3815801.33
Authors
Ishiguro, K.,Yokoyama, T.,Shirouzu, M.,Suzuki, T. (deposition date: 2023-05-14, release date: 2023-12-06, Last modification date: 2025-02-12)
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 (2.26 Å)
Structure validation

237735

数据于2025-06-18公开中

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