Ribosome interactions of aminoacyl-tRNA and elongation factor Tu in the codon-recognition complex

Nat Struct Biol. 2002 Nov;9(11):849-54. doi: 10.1038/nsb859.

Abstract

The mRNA codon in the ribosomal A-site is recognized by aminoacyl-tRNA (aa-tRNA) in a ternary complex with elongation factor Tu (EF-Tu) and GTP. Here we report the 13 A resolution three-dimensional reconstruction determined by cryo-electron microscopy of the kirromycin-stalled codon-recognition complex. The structure of the ternary complex is distorted by binding of the tRNA anticodon arm in the decoding center. The aa-tRNA interacts with 16S rRNA, helix 69 of 23S rRNA and proteins S12 and L11, while the sarcin-ricin loop of 23S rRNA contacts domain 1 of EF-Tu near the nucleotide-binding pocket. These results provide a detailed snapshot view of an important functional state of the ribosome and suggest mechanisms of decoding and GTPase activation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Codon / metabolism*
  • Escherichia coli
  • Macromolecular Substances
  • Nucleic Acid Conformation
  • Peptide Elongation Factor Tu / metabolism*
  • Protein Biosynthesis / physiology*
  • Protein Structure, Tertiary
  • RNA, Transfer, Amino Acyl / metabolism*
  • Ribosomes / metabolism*
  • Ribosomes / ultrastructure

Substances

  • Codon
  • Macromolecular Substances
  • RNA, Transfer, Amino Acyl
  • Peptide Elongation Factor Tu

Associated data

  • PDB/1MJ1