4V6F
Elongation complex of the 70S ribosome with three tRNAs and mRNA.
This is a non-PDB format compatible entry.
Summary for 4V6F
| Entry DOI | 10.2210/pdb4v6f/pdb |
| Related | 3I8G 3I8H 3I8I |
| Descriptor | 23S RIBOSOMAL RNA, 50S RIBOSOMAL PROTEIN L14, 50S RIBOSOMAL PROTEIN L15, ... (61 entities in total) |
| Functional Keywords | ribosome, trna, mrna |
| Biological source | Thermus thermophilus More |
| Total number of polymer chains | 114 |
| Total formula weight | 4678968.83 |
| Authors | Jenner, L.B.,Yusupova, G.,Yusupov, M. (deposition date: 2009-07-09, release date: 2014-07-09, Last modification date: 2024-11-06) |
| Primary citation | Jenner, L.B.,Demeshkina, N.,Yusupova, G.,Yusupov, M. Structural aspects of messenger RNA reading frame maintenance by the ribosome. Nat.Struct.Mol.Biol., 17:555-560, 2010 Cited by PubMed Abstract: One key question in protein biosynthesis is how the ribosome couples mRNA and tRNA movements to prevent disruption of weak codon-anticodon interactions and loss of the translational reading frame during translocation. Here we report the complete path of mRNA on the 70S ribosome at the atomic level (3.1-A resolution), and we show that one of the conformational rearrangements that occurs upon transition from initiation to elongation is a narrowing of the downstream mRNA tunnel. This rearrangement triggers formation of a network of interactions between the mRNA downstream of the A-site codon and the elongating ribosome. Our data elucidate the mechanism by which hypermodified nucleoside 2-methylthio-N6 isopentenyl adenosine at position 37 (ms(2)i(6)A37) in tRNA(Phe)(GAA) stabilizes mRNA-tRNA interactions in all three tRNA binding sites. Another network of contacts is formed between this tRNA modification and ribosomal elements surrounding the mRNA E/P kink, resulting in the anchoring of P-site tRNA. These data allow rationalization of how modification deficiencies of ms(2)i(6)A37 in tRNAs may lead to shifts of the translational reading frame. PubMed: 20400952DOI: 10.1038/nsmb.1790 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.1 Å) |
Structure validation
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