Mechanisms of colicin binding and transport through outer membrane porins.

  title={Mechanisms of colicin binding and transport through outer membrane porins.},
  author={Zhenghua Cao and Phillip E. Klebba},
  volume={84 5-6},
To kill Escherichia coli, toxic proteins, called colicins, pass through the permeability barrier created by the outer membrane (OM) of the bacterial cell envelope. We consider a variety of different colicins, including A, B, D, E1, E3, Ia, M and N, that penetrate through the porins OmpF, FepA, BtuB, Cir and FhuA, to subsequently interact with a few targets in the periplasm, including TolA, TolB, TolC and TonB. We review the mechanisms, demonstrated and postulated, by which such toxins enter… CONTINUE READING


Publications citing this paper.
Showing 1-10 of 37 extracted citations


Publications referenced by this paper.
Showing 1-10 of 122 references

Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein

  • V. Koronakis
  • export, Nature
  • 2000
Highly Influential
5 Excerpts

Structure of the Escherichia coli TolB protein determined by MAD methods at 1.95 A resolution, Structure Fold Des

  • C. Abergel
  • 1999
Highly Influential
4 Excerpts

Crystal structure of colicin Ia, Nature

  • M. Wiener
  • 1997
Highly Influential
4 Excerpts

Structural basis for sugar translocation through maltoporin channels at 3.1 A resolution, Science

  • T. Schirmer
  • 1995
Highly Influential
4 Excerpts

Similar Papers

Loading similar papers…