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4V6G

Initiation complex of 70S ribosome with two tRNAs and mRNA.

This is a non-PDB format compatible entry.
Summary for 4V6G
Entry DOI10.2210/pdb4v6g/pdb
Related3I8F 3I8G 3I8H 3I8I 3I9C 3I9D 3I9E
Descriptor16S RRNA (E.COLI NUMBERING), 30S RIBOSOMAL PROTEIN S10, 30S RIBOSOMAL PROTEIN S11, ... (55 entities in total)
Functional Keywordsribosome, trna, mrna
Biological sourceThermus thermophilus
More
Total number of polymer chains109
Total formula weight4520213.78
Authors
Jenner, L.B.,Yusupova, G.,Yusupov, M. (deposition date: 2009-07-10, release date: 2014-07-09, Last modification date: 2024-12-25)
Primary citationJenner, 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: 20400952
DOI: 10.1038/nsmb.1790
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.5 Å)
Structure validation

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