8G7S
Structure of the Escherichia coli 70S ribosome in complex with P-site tRNAIle(LAU) bound to the cognate AUA codon (Structure IV)
This is a non-PDB format compatible entry.
Summary for 8G7S
| Entry DOI | 10.2210/pdb8g7s/pdb |
| EMDB information | 29822 |
| Descriptor | 16S Ribosomal RNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (58 entities in total) |
| Functional Keywords | lysidine 34, cryo-em, trna, ribosome |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 55 |
| Total formula weight | 2208115.69 |
| Authors | Rybak, M.Y.,Gagnon, M.G. (deposition date: 2023-02-16, release date: 2024-03-06, Last modification date: 2024-05-29) |
| Primary citation | Rybak, M.Y.,Gagnon, M.G. Structures of the ribosome bound to EF-Tu-isoleucine tRNA elucidate the mechanism of AUG avoidance. Nat.Struct.Mol.Biol., 31:810-816, 2024 Cited by PubMed Abstract: The frequency of errors upon decoding of messenger RNA by the bacterial ribosome is low, with one misreading event per 1 × 10 codons. In the universal genetic code, the AUN codon box specifies two amino acids, isoleucine and methionine. In bacteria and archaea, decoding specificity of the AUA and AUG codons relies on the wobble avoidance strategy that requires modification of C34 in the anticodon loop of isoleucine transfer RNA (tRNA). Bacterial tRNA with 2-lysylcytidine (lysidine) at the wobble position deciphers AUA while avoiding AUG. Here we report cryo-electron microscopy structures of the Escherichia coli 70S ribosome complexed with elongation factor thermo unstable (EF-Tu) and isoleucine-tRNA in the process of decoding AUA and AUG. Lysidine in tRNA excludes AUG by promoting the formation of an unusual Hoogsteen purine-pyrimidine nucleobase geometry at the third position of the codon, weakening the interactions with the mRNA and destabilizing the EF-Tu ternary complex. Our findings elucidate the molecular mechanism by which tRNA specifically decodes AUA over AUG. PubMed: 38538914DOI: 10.1038/s41594-024-01236-3 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.1 Å) |
Structure validation
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