The ternary complex of aminoacylated tRNA and EF-Tu-GTP. Recognition of a bond and a fold.

@article{Nissen1996TheTC,
  title={The ternary complex of aminoacylated tRNA and EF-Tu-GTP. Recognition of a bond and a fold.},
  author={Poul Nissen and Morten Kjeldgaard and S\oren Thirup and Brian F. C. Clark and Jens Nyborg},
  journal={Biochimie},
  year={1996},
  volume={78 11-12},
  pages={921-33}
}
The refined crystal structure of the ternary complex of yeast Phe-tRNAPhe, Thermus aquaticus elongation factor EF-Tu and the non-hydrolyzable GTP analog, GDPNP, reveals many details of the EF-Tu recognition of aminoacylated tRNA (aa-tRNA). EF-Tu-GTP recognizes the aminoacyl bond and one side of the backbone fold of the acceptor helix and has a high affinity for all ordinary elongator aa-tRNAs by binding to this aa-tRNA motif. Yet, the binding of deacylated tRNA, initiator tRNA, and… CONTINUE READING

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