Ribosome interactions of aminoacyl-tRNA and elongation factor Tu in the codon-recognition complex

被引：166

作者：

Stark, H ^{[1
]}

Rodnina, MV

Wieden, HJ

Zemlin, F

Wintermeyer, W

van Heel, M

机构：

[1] Max Planck Inst Biophys Chem, D-37077 Gottingen, Germany

[2] Univ Witten Herdecke, Inst Phys Biochem, D-58448 Witten, Germany

[3] Max Planck Soc, Fritz Haber Inst, D-14195 Berlin, Germany

[4] Univ Witten Herdecke, Inst Mol Biol, D-58448 Witten, Germany

[5] Univ London Imperial Coll Sci Technol & Med, Dept Biol Sci, London SW7 2AY, England

来源：

NATURE STRUCTURAL BIOLOGY | 2002年 / 9卷 / 11期

基金：

英国生物技术与生命科学研究理事会;

关键词：

D O I：

10.1038/nsb859

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The mRNA codon in the ribosomal A-site is recognized by aminoacyl-tRNA (aa-tRNA) in a ternary complex with elongation factor Tu (EF-Tu) and GTP. Here we report the 13 Angstrom resolution three-dimensional reconstruction determined by cryo-electron microscopy of the kirromycin-stalled codon-recognition complex. The structure of the ternary complex is distorted by binding of the tRNA anticodon arm in the decoding center. The aa-tRNA interacts with 16S rRNA, helix 69 of 23S rRNA and proteins S12 and L11, while the sarcin-ricin loop of 23S rRNA contacts domain 1 of EF-Tu near the nucleotide-binding pocket. These results provide a detailed snapshot view of an important functional state of the ribosome and suggest mechanisms of decoding and GTPase activation.

引用

页码：849 / 854

页数：6

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