Molecular basis for the ribosome functioning as an L-tryptophan sensor.

@article{Bischoff2014MolecularBF,
  title={Molecular basis for the ribosome functioning as an L-tryptophan sensor.},
  author={Lukas Bischoff and Otto Berninghausen and Roland Beckmann},
  journal={Cell reports},
  year={2014},
  volume={9 2},
  pages={469-75}
}
Elevated levels of the free amino acid L-tryptophan (L-Trp) trigger expression of the tryptophanase tnaCAB operon in E. coli. Activation depends on tryptophan-dependent ribosomal stalling during translation of the upstream TnaC peptide. Here, we present a cryoelectron microscopy (cryo-EM) reconstruction at 3.8 Å resolution of a ribosome stalled by the TnaC peptide. Unexpectedly, we observe two L-Trp molecules in the ribosomal exit tunnel coordinated within composite hydrophobic pockets formed… CONTINUE READING
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