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4WT1

Complex of 70S ribosome with tRNA-Phe and mRNA with A-A mismatch in the second position in the A-site

This is a non-PDB format compatible entry.
Summary for 4WT1
Entry DOI10.2210/pdb4wt1/pdb
Descriptor16S ribosomal RNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (58 entities in total)
Functional Keywordsribosome, translation, mismatch
Biological sourceThermus thermophilus HB8
More
Total number of polymer chains110
Total formula weight4526292.47
Authors
Rozov, A.,Demeshkina, N.,Yusupov, M.,Yusupova, G. (deposition date: 2014-10-29, release date: 2015-06-10, Last modification date: 2024-10-16)
Primary citationRozov, 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: 26037619
DOI: 10.1038/ncomms8251
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.05 Å)
Structure validation

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