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TitleRecognition of aminoacyl-tRNA: a common molecular mechanism revealed by cryo-EM.
Journal, issue, pagesEMBO J, Vol. 27, Issue 24, Page 3322-3331, Year 2008
Publish dateDec 17, 2008
AuthorsWen Li / Xabier Agirrezabala / Jianlin Lei / Lamine Bouakaz / Julie L Brunelle / Rodrigo F Ortiz-Meoz / Rachel Green / Suparna Sanyal / Måns Ehrenberg / Joachim Frank /
PubMed AbstractThe 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 ...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.
External linksEMBO J / PubMed:19020518 / PubMed Central
MethodsEM (single particle)
Resolution9.0 - 12.0 Å
Structure data

1564

3eq4

EMDB-1564: Recognition of Phe-tRNAPhe, Trp-tRNATrp and : a common molecular mechanism for aminoacyl-tRNA selection revealed by cryo-EM
PDB-3eq4: Model of tRNA(Leu)-EF-Tu in the ribosomal pre-accommodated state revealed by cryo-EM
Method: EM (single particle) / Resolution: 12.0 Å

1565

3eq3

EMDB-1565: Recognition of Phe-tRNAPhe, Trp-tRNATrp and : a common molecular mechanism for aminoacyl-tRNA selection revealed by cryo-EM
PDB-3eq3: Model of tRNA(Trp)-EF-Tu in the ribosomal pre-accommodated state revealed by cryo-EM
Method: EM (single particle) / Resolution: 9.0 Å

PDB-3ep2:
Model of Phe-tRNA(Phe) in the ribosomal pre-accommodated state revealed by cryo-EM
Method: ELECTRON MICROSCOPY / Resolution: 9 Å

Source
  • Escherichia coli (E. coli)
  • escherichia coli k12 (bacteria)
KeywordsRIBOSOMAL PROTEIN/RNA / protein translation / ternary complex / A/T-tRNA / automated data collection / Antibiotic resistance / Elongation factor / GTP-binding / Membrane / Methylation / Nucleotide-binding / Phosphoprotein / Protein biosynthesis / Ribonucleoprotein / Ribosomal protein / RNA-binding / rRNA-binding / tRNA-binding / RIBOSOMAL PROTEIN-RNA COMPLEX

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