8BGH
Elongating E. coli 70S ribosome containing acylated tRNA(iMet) in the P-site and AAA mRNA codon in the A-site after uncompleted di-peptide formation
This is a non-PDB format compatible entry.
Summary for 8BGH
| Entry DOI | 10.2210/pdb8bgh/pdb |
| Related | 8BF7 8BGE |
| EMDB information | 16015 16029 16031 |
| Descriptor | 50S ribosomal protein L2, 50S ribosomal protein L16, 50S ribosomal protein L17, ... (55 entities in total) |
| Functional Keywords | m6a, mrna modification, trna recognition, translation |
| Biological source | Escherichia coli K-12 More |
| Total number of polymer chains | 54 |
| Total formula weight | 2174247.20 |
| Authors | |
| Primary citation | Jain, S.,Koziej, L.,Poulis, P.,Kaczmarczyk, I.,Gaik, M.,Rawski, M.,Ranjan, N.,Glatt, S.,Rodnina, M.V. Modulation of translational decoding by m 6 A modification of mRNA. Nat Commun, 14:4784-4784, 2023 Cited by PubMed Abstract: N-methyladenosine (mA) is an abundant, dynamic mRNA modification that regulates key steps of cellular mRNA metabolism. mA in the mRNA coding regions inhibits translation elongation. Here, we show how mA modulates decoding in the bacterial translation system using a combination of rapid kinetics, smFRET and single-particle cryo-EM. We show that, while the modification does not impair the initial binding of aminoacyl-tRNA to the ribosome, in the presence of mA fewer ribosomes complete the decoding process due to the lower stability of the complexes and enhanced tRNA drop-off. The mRNA codon adopts a π-stacked codon conformation that is remodeled upon aminoacyl-tRNA binding. mA does not exclude canonical codon-anticodon geometry, but favors alternative more dynamic conformations that are rejected by the ribosome. These results highlight how modifications outside the Watson-Crick edge can still interfere with codon-anticodon base pairing and complex recognition by the ribosome, thereby modulating the translational efficiency of modified mRNAs. PubMed: 37553384DOI: 10.1038/s41467-023-40422-7 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.88 Å) |
Structure validation
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