The crystal structure of ribosomal chaperone trigger factor from Vibrio cholerae.

@article{Ludlam2004TheCS,
  title={The crystal structure of ribosomal chaperone trigger factor from Vibrio cholerae.},
  author={Anthony V Ludlam and Brian A Moore and Zhaohui Xu},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2004},
  volume={101 37},
  pages={13436-41}
}
Trigger factor is a molecular chaperone that is present in all species of eubacteria. It binds to the ribosomal 50S subunit near the translation exit tunnel and is thought to be the first protein to interact with nascent polypeptides emerging from the ribosome. The chaperone has a peptidyl-prolyl cis-trans isomerase (PPIase) activity that catalyzes the rate-limiting proline isomerization in the protein-folding process. We have determined the crystal structure of nearly full-length trigger… CONTINUE READING
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