PMID:12379845

Citation	Stark, H, Rodnina, MV, Wieden, HJ, Zemlin, F, Wintermeyer, W and van Heel, M (2002) Ribosome interactions of aminoacyl-tRNA and elongation factor Tu in the codon-recognition complex. Nat. Struct. Biol. 9:849-54
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.
Links	PubMed Online version:10.1038/nsb859
Keywords	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
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