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TitleRibosome rearrangements at the onset of translational bypassing.
Journal, issue, pagesSci Adv, Vol. 3, Issue 6, Page e1700147, Year 2017
Publish dateJun 7, 2017
AuthorsXabier Agirrezabala / Ekaterina Samatova / Mariia Klimova / Miguel Zamora / David Gil-Carton / Marina V Rodnina / Mikel Valle /
PubMed AbstractBypassing is a recoding event that leads to the translation of two distal open reading frames into a single polypeptide chain. We present the structure of a translating ribosome stalled at the ...Bypassing is a recoding event that leads to the translation of two distal open reading frames into a single polypeptide chain. We present the structure of a translating ribosome stalled at the bypassing take-off site of of bacteriophage T4. The nascent peptide in the exit tunnel anchors the P-site peptidyl-tRNA to the ribosome and locks an inactive conformation of the peptidyl transferase center (PTC). The mRNA forms a short dynamic hairpin in the decoding site. The ribosomal subunits adopt a rolling conformation in which the rotation of the small subunit around its long axis causes the opening of the A-site region. Together, PTC conformation and mRNA structure safeguard against premature termination and read-through of the stop codon and reconfigure the ribosome to a state poised for take-off and sliding along the noncoding mRNA gap.
External linksSci Adv / PubMed:28630923 / PubMed Central
MethodsEM (single particle)
Resolution3.6 Å
Structure data

3618

5np6

EMDB-3618: Bypassing 70S ribosome
PDB-5np6: 70S structure prior to bypassing
Method: EM (single particle) / Resolution: 3.6 Å

Source
  • escherichia coli (E. coli)
  • enterobacteria phage t4 (virus)
  • escherichia coli (strain k12) (bacteria)
KeywordsRIBOSOME / translation / bypassing / protein

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