Structure-Function Relationships of a Novel Bacterial Toxin, Hemolysin E

@article{Atkins2000StructureFunctionRO,
  title={Structure-Function Relationships of a Novel Bacterial Toxin, Hemolysin E},
  author={A. Atkins and N. R. Wyborn and A. J. Wallace and T. J. Stillman and L. K. Black and A. Fielding and M. Hisakado and P. Artymiuk and J. Green},
  journal={The Journal of Biological Chemistry},
  year={2000},
  volume={275},
  pages={41150 - 41155}
}
The novel pore-forming toxin hemolysin E (HlyE, ClyA, or SheA) consists of a long four-helix bundle with a subdomain (β tongue) that interacts with target membranes at one pole and an additional helix (αG) that, with the four long helices, forms a five-helix bundle (tail domain) at the other pole. Random amino acid substitutions that impair hemolytic activity were clustered mostly, but not exclusively, within the tail domain, specifically amino acids within, adjacent to, or interacting with αG… Expand
Mutations affecting export and activity of cytolysin A from Escherichia coli.
Assembly mechanism of the α-pore–forming toxin cytolysin A from Escherichia coli
Properties of haemolysin E (HlyE) from a pathogenic Escherichia coli avian isolate and studies of HlyE export.
The formation and structure of Escherichia coli K-12 haemolysin E pores.
Structure of the Hemolysin E (HlyE, ClyA, and SheA) Channel in Its Membrane-bound Form*
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