Acidic pH-induced membrane insertion of colicin A into E. coli natural lipids probed by site-directed spin labeling.

@article{Pulagam2013AcidicPM,
  title={Acidic pH-induced membrane insertion of colicin A into E. coli natural lipids probed by site-directed spin labeling.},
  author={Lakshmi Padmavathi Pulagam and Heinz-J{\"u}rgen Steinhoff},
  journal={Journal of molecular biology},
  year={2013},
  volume={425 10},
  pages={
          1782-94
        }
}
Colicin A is a pore-forming toxin that forms a voltage-gated channel in the inner membrane of the target bacteria. The structures of the closed and open channel states of membrane-bound colicin A are not resolved. In the present site-directed spin-labeling study, the insertion-competent state of colicin A is provoked by an acidic pH jump prior to the insertion into liposomes prepared from Escherichia coli natural lipids. The membrane-bound colicin A is able to open a voltage-dependent channel… CONTINUE READING

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