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The accuracy of ribosomal translation is achieved by an initial selection and a proofreading step, mediated by EF-Tu, which forms a ternary complex with aminoacyl(aa)-tRNA. To study the binding modes of different aa-tRNAs, we compared cryo-EM maps of the kirromycin-stalled ribosome bound with ternary complexes containing Phe-tRNA(Phe), Trp-tRNA(Trp), or Leu-tRNA(LeuI). The three maps suggest a common binding manner of cognate aa-tRNAs in their specific binding with both the ribosome and EF-Tu. All three aa-tRNAs have the same 'loaded spring' conformation with a kink and twist between the D-stem and anticodon stem. The three complexes are similarly integrated in an interaction network, extending from the anticodon loop through h44 and protein S12 to the EF-Tu-binding CCA end of aa-tRNA, proposed to signal cognate codon-anticodon interaction to the GTPase centre and tune the accuracy of aa-tRNA selection.

Recognition of aminoacyl-tRNA: a common molecular mechanism revealed by cryo-EM., Li W, Agirrezabala X, Lei J, Bouakaz L, Brunelle JL, Ortiz-Meoz RF, Green R, Sanyal S, Ehrenberg M, Frank J, EMBO J. 2008 Dec 17;27(24):3322-31. Epub 2008 Nov 20. PMID:19020518

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Categories: Escherichia coli k12 | Agirrezabala, X. | Frank, J. | Li, W. | A/t-trna | Acetylation | Antibiotic resistance | Automated data collection | Cytoplasm | Elongation factor | Gtp-binding | Membrane | Methylation | Nucleotide-binding | Phosphoprotein | Protein biosynthesis | Protein translation | Ribonucleoprotein | Ribosomal protein | Ribosomal protein/rna complex | Rna-binding | Rrna-binding | Ternary complex | Trna-binding