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-Structure paper
Title | Ribosome rearrangements at the onset of translational bypassing. |
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Journal, issue, pages | Sci Adv, Vol. 3, Issue 6, Page e1700147, Year 2017 |
Publish date | Jun 7, 2017 |
Authors | Xabier Agirrezabala / Ekaterina Samatova / Mariia Klimova / Miguel Zamora / David Gil-Carton / Marina V Rodnina / Mikel Valle / |
PubMed Abstract | 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 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 links | Sci Adv / PubMed:28630923 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.6 Å |
Structure data | |
Source |
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Keywords | RIBOSOME / translation / bypassing / protein |