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

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Stark,  H.
Research Group of 3D Electron Cryo-Microscopy, MPI for biophysical chemistry, Max Planck Society;

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Wintermeyer,  W.
Research Group of Ribosome Dynamics, MPI for biophysical chemistry, Max Planck Society;

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Citation

Stark, H., Rodnina, M. V., Wieden, H. J., Zemlin, F., Wintermeyer, W., & van Heel, M. (2002). Ribosome interactions of aminoacyl-tRNA and elongation factor Tu in the codon-recognition complex. Nature Structural Biology, 9(11), 849-854. Retrieved from http://www.nature.com/nsmb/journal/v9/n11/pdf/nsb859.pdf.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002D-4541-B
Abstract
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.