3EQ3

Model of tRNA(Trp)-EF-Tu in the ribosomal pre-accommodated state revealed by cryo-EM

Summary for 3EQ3

• Entry DOI: 10.2210/pdb3eq3/pdb
• Related: 1OB2 1QZA 2AVY 2AW4 3EP2 3EQ4
• EMDB information: 1564 1565
• Descriptor: Elongation factor Tu, 30S ribosomal protein S12, 50S ribosomal protein L11, ... (9 entities in total)
• Functional Keywords: 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, ribosomal protein/rna
• Biological source: Escherichia coli K12; More
• Total number of polymer chains: 9
• Total formula weight: 131977.58

Authors

Frank, J.,Li, W.,Agirrezabala, X. (deposition date: 2008-09-30, release date: 2008-12-16, Last modification date: 2024-02-21)

Primary citation

Li, W.,Agirrezabala, X.,Lei, J.,Bouakaz, L.,Brunelle, J.L.,Ortiz-Meoz, R.F.,Green, R.,Sanyal, S.,Ehrenberg, M.,Frank, J.
Recognition of aminoacyl-tRNA: a common molecular mechanism revealed by cryo-EM.
Embo J., 27:3322-3331, 2008

PubMed Abstract: 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.

PubMed: 19020518
DOI: 10.1038/emboj.2008.243

Experimental method

ELECTRON MICROSCOPY (9 Å)