4WQ1
Complex of 70S ribosome with tRNA-Tyr and mRNA with C-A mismatch in the first position in the A-site.
This is a non-PDB format compatible entry.
Summary for 4WQ1
Entry DOI | 10.2210/pdb4wq1/pdb |
Descriptor | 16S ribosomal RNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (62 entities in total) |
Functional Keywords | ribosome, translation, mismatch |
Biological source | Thermus thermophilus HB8 More |
Total number of polymer chains | 110 |
Total formula weight | 4519200.77 |
Authors | Rozov, A.,Demeshkina, N.,Yusupov, M.,Yusupova, G. (deposition date: 2014-10-21, release date: 2015-06-10, Last modification date: 2024-10-23) |
Primary citation | Rozov, A.,Demeshkina, N.,Westhof, E.,Yusupov, M.,Yusupova, G. Structural insights into the translational infidelity mechanism. Nat Commun, 6:7251-7251, 2015 Cited by PubMed Abstract: The decoding of mRNA on the ribosome is the least accurate process during genetic information transfer. Here we propose a unified decoding mechanism based on 11 high-resolution X-ray structures of the 70S ribosome that explains the occurrence of missense errors during translation. We determined ribosome structures in rare states where incorrect tRNAs were incorporated into the peptidyl-tRNA-binding site. These structures show that in the codon-anticodon duplex, a G·U mismatch adopts the Watson-Crick geometry, indicating a shift in the tautomeric equilibrium or ionization of the nucleobase. Additional structures with mismatches in the 70S decoding centre show that the binding of any tRNA induces identical rearrangements in the centre, which favours either isosteric or close to the Watson-Crick geometry codon-anticodon pairs. Overall, the results suggest that a mismatch escapes discrimination by preserving the shape of a Watson-Crick pair and indicate that geometric selection via tautomerism or ionization dominates the translational infidelity mechanism. PubMed: 26037619DOI: 10.1038/ncomms8251 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.1 Å) |
Structure validation
Download full validation report