Ribosome interactions of aminoacyl-tRNA and elongation factor Tu in the codon-recognition complex.
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Stark H, Rodnina MV, Wieden HJ, Zemlin F, Wintermeyer W, van Heel M
Ribosome interactions of aminoacyl-tRNA and elongation factor Tu in the codon-recognition complex.
Nat Struct Biol. 2002 Nov;9(11):849-54.
- PubMed ID
- 12379845 [ View in PubMed]
- 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.