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-Structure paper
タイトル | Recognition of aminoacyl-tRNA: a common molecular mechanism revealed by cryo-EM. |
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ジャーナル・号・ページ | EMBO J, Vol. 27, Issue 24, Page 3322-3331, Year 2008 |
掲載日 | 2008年12月17日 |
![]() | Wen Li / Xabier Agirrezabala / Jianlin Lei / Lamine Bouakaz / Julie L Brunelle / Rodrigo F Ortiz-Meoz / Rachel Green / Suparna Sanyal / Måns Ehrenberg / Joachim Frank / ![]() |
PubMed 要旨 | 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 ...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. |
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手法 | EM (単粒子) |
解像度 | 9.0 - 12.0 Å |
構造データ | EMDB-1564: Recognition of Phe-tRNAPhe, Trp-tRNATrp and : a common molecular mechanism for aminoacyl-tRNA selection revealed by cryo-EM EMDB-1565: Recognition of Phe-tRNAPhe, Trp-tRNATrp and : a common molecular mechanism for aminoacyl-tRNA selection revealed by cryo-EM ![]() PDB-3ep2: |
由来 |
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![]() | RIBOSOMAL 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 |