5D8B
Crystal structure of T. thermophilus ribosome containing a P-site wobble mismatch
This is a non-PDB format compatible entry.
Summary for 5D8B
Entry DOI | 10.2210/pdb5d8b/pdb |
Descriptor | 50S ribosomal protein L2, 50S ribosomal protein L15, 50S ribosomal protein L16, ... (56 entities in total) |
Functional Keywords | non-aug initiation, wobble mismatch, cytosine-cytosine mismatch, ribosome, translation |
Biological source | Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039) More |
Total number of polymer chains | 110 |
Total formula weight | 4505462.70 |
Authors | Svidritskiy, E.,Korostelev, A.A. (deposition date: 2015-08-17, release date: 2015-10-14, Last modification date: 2023-09-27) |
Primary citation | Svidritskiy, E.,Korostelev, A.A. Ribosome Structure Reveals Preservation of Active Sites in the Presence of a P-Site Wobble Mismatch. Structure, 23:2155-2161, 2015 Cited by PubMed Abstract: Translation initiation in the P site occasionally occurs at atypical (non-AUG) start codons, including those forming a mismatch in the third (wobble) position. During elongation, however, a pyrimidine-pyrimidine wobble mismatch may trigger a translation quality-control mechanism, whereby the P-site mismatch is thought to perturb the downstream A-site codon or the decoding center, thereby reducing translation fidelity and inducing termination of aberrant translation. We report a crystal structure of the 70S initiation complex containing an AUC codon in the ribosomal P site. Remarkably, the ribosome stabilizes the mismatched codon-anticodon helix, arranging a normally disruptive cytosine-cytosine pair into a Watson-Crick-like conformation. Translation-competent conformations of the tRNA, mRNA, and decoding center suggest that a P-site wobble-position mismatch in the 70S initiation complex does not pre-arrange the mRNA or decoding center to favor subsequent miscoding events. PubMed: 26412335DOI: 10.1016/j.str.2015.08.011 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.63 Å) |
Structure validation
Download full validation report
