5EL7

Structure of T. thermophilus 70S ribosome complex with mRNA and tRNALys in the A-site with a U-U mismatch in the second position and antibiotic paromomycin

This is a non-PDB format compatible entry.

Summary for 5EL7

• Entry DOI: 10.2210/pdb5el7/pdb
• Descriptor: 16S rRNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (61 entities in total)
• Functional Keywords: translation, ribosome, mismatch
• Biological source: Thermus thermophilus HB8; More
• Total number of polymer chains: 109
• Total formula weight: 4556592.28

Authors

Rozov, A.,Demeshkina, N.,Khusainov, I.,Yusupov, M.,Yusupova, G. (deposition date: 2015-11-04, release date: 2016-01-27, Last modification date: 2024-01-10)

Primary citation

Rozov, A.,Demeshkina, N.,Khusainov, I.,Westhof, E.,Yusupov, M.,Yusupova, G.
Novel base-pairing interactions at the tRNA wobble position crucial for accurate reading of the genetic code.
Nat Commun, 7:10457-10457, 2016

PubMed Abstract: Posttranscriptional modifications at the wobble position of transfer RNAs play a substantial role in deciphering the degenerate genetic code on the ribosome. The number and variety of modifications suggest different mechanisms of action during messenger RNA decoding, of which only a few were described so far. Here, on the basis of several 70S ribosome complex X-ray structures, we demonstrate how Escherichia coli tRNA(Lys)(UUU) with hypermodified 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position discriminates between cognate codons AAA and AAG, and near-cognate stop codon UAA or isoleucine codon AUA, with which it forms pyrimidine-pyrimidine mismatches. We show that mnm(5)s(2)U forms an unusual pair with guanosine at the wobble position that expands general knowledge on the degeneracy of the genetic code and specifies a powerful role of tRNA modifications in translation. Our models consolidate the translational fidelity mechanism proposed previously where the steric complementarity and shape acceptance dominate the decoding mechanism.

PubMed: 26791911
DOI: 10.1038/ncomms10457

Experimental method

X-RAY DIFFRACTION (3.15 Å)