Identification and characterization of an amphipathic leucine zipper-like motif in Escherichia coli toxin hemolysin E. Plausible role in the assembly and membrane destabilization.

@article{Yadav2003IdentificationAC,
  title={Identification and characterization of an amphipathic leucine zipper-like motif in Escherichia coli toxin hemolysin E. Plausible role in the assembly and membrane destabilization.},
  author={Sharada Prasad Yadav and Bijoy Kundu and Jimut Kanti Ghosh},
  journal={The Journal of biological chemistry},
  year={2003},
  volume={278 51},
  pages={
          51023-34
        }
}
Hemolysin E (HlyE) is a 34 kDa protein toxin, recently isolated from a pathogenic strain of Escherichia coli, which is believed to exert its toxic activity via formation of pores in the target cell membrane. With the goal of understanding the involvement of different segments of hemolysin E in the membrane interaction and assembly of the toxin, a conserved, amphipathic leucine zipper-like motif has been identified. In order to evaluate the possible structural and functional roles of this… CONTINUE READING
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