Cysteine-scanning mutagenesis and disulfide mapping studies of the conserved domain of the twin-arginine translocase TatB component.

@article{Lee2006CysteinescanningMA,
  title={Cysteine-scanning mutagenesis and disulfide mapping studies of the conserved domain of the twin-arginine translocase TatB component.},
  author={Philip S. Lee and George L. Orriss and Grant Buchanan and Nicholas P Greene and Peter J. Bond and Claire Punginelli and Rachael L Jack and Mark S. P. Sansom and Ben C Berks and Tracy Palmer},
  journal={The Journal of biological chemistry},
  year={2006},
  volume={281 45},
  pages={34072-85}
}
The cytoplasmic membrane protein TatB is an essential component of the Escherichia coli twin-arginine (Tat) protein translocation pathway. Together with the TatC component it forms a complex that functions as a membrane receptor for substrate proteins. Structural predictions suggest that TatB is anchored to the membrane via an N-terminal transmembrane alpha-helix that precedes an amphipathic alpha-helical section of the protein. From truncation analysis it is known that both these regions of… CONTINUE READING

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