The conformation of a signal peptide bound by Escherichia coli preprotein translocase SecA.

@article{Chou2005TheCO,
  title={The conformation of a signal peptide bound by Escherichia coli preprotein translocase SecA.},
  author={Yi-Te Chou and Lila M. Gierasch},
  journal={The Journal of biological chemistry},
  year={2005},
  volume={280 38},
  pages={32753-60}
}
To understand the structural nature of signal sequence recognition by the preprotein translocase SecA, we have characterized the interactions of a signal peptide corresponding to a LamB signal sequence (modified to enhance aqueous solubility) with SecA by NMR methods. One-dimensional NMR studies showed that the signal peptide binds SecA with a moderately fast exchange rate (Kd approximately 10(-5) m). The line-broadening effects observed from one-dimensional and two-dimensional NMR spectra… CONTINUE READING

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