6DNC
E.coli RF1 bound to E.coli 70S ribosome in response to UAU sense A-site codon
This is a non-PDB format compatible entry.
Summary for 6DNC
| Entry DOI | 10.2210/pdb6dnc/pdb |
| EMDB information | 7970 |
| Descriptor | 16S ribosomal RNA, 50S ribosomal protein L6, 50S ribosomal protein L9, ... (58 entities in total) |
| Functional Keywords | rf1, ribosome, sense codon, cryo-em |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 59 |
| Total formula weight | 2292649.20 |
| Authors | Svidritskiy, E.,Demo, G.,Korostelev, A.A. (deposition date: 2018-06-06, release date: 2018-07-04, Last modification date: 2024-03-13) |
| Primary citation | Svidritskiy, E.,Demo, G.,Korostelev, A.A. Mechanism of premature translation termination on a sense codon. J. Biol. Chem., 293:12472-12479, 2018 Cited by PubMed Abstract: Accurate translation termination by release factors (RFs) is critical for the integrity of cellular proteomes. Premature termination on sense codons, for example, results in truncated proteins, whose accumulation could be detrimental to the cell. Nevertheless, some sense codons are prone to triggering premature termination, but the structural basis for this is unclear. To investigate premature termination, we determined a cryo-EM structure of the 70S ribosome bound with RF1 in response to a UAU (Tyr) sense codon. The structure reveals that RF1 recognizes a UAU codon similarly to a UAG stop codon, suggesting that sense codons induce premature termination because they structurally mimic a stop codon. Hydrophobic interaction between the nucleobase of U3 (the third position of the UAU codon) and conserved Ile-196 in RF1 is important for misreading the UAU codon. Analyses of RNA binding in ribonucleoprotein complexes or by amino acids reveal that Ile-U packing is a frequent protein-RNA-binding motif with key functional implications. We discuss parallels with eukaryotic translation termination by the release factor eRF1. PubMed: 29941456DOI: 10.1074/jbc.AW118.003232 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.7 Å) |
Structure validation
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