3EQ3
Model of tRNA(Trp)-EF-Tu in the ribosomal pre-accommodated state revealed by cryo-EM
3EQ3 の概要
| エントリーDOI | 10.2210/pdb3eq3/pdb |
| 関連するPDBエントリー | 1OB2 1QZA 2AVY 2AW4 3EP2 3EQ4 |
| EMDBエントリー | 1564 1565 |
| 分子名称 | Elongation factor Tu, 30S ribosomal protein S12, 50S ribosomal protein L11, ... (9 entities in total) |
| 機能のキーワード | 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 |
| 由来する生物種 | Escherichia coli K12 詳細 |
| タンパク質・核酸の鎖数 | 9 |
| 化学式量合計 | 131977.58 |
| 構造登録者 | |
| 主引用文献 | 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 Cited by 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: 19020518DOI: 10.1038/emboj.2008.243 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (9 Å) |
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