Crystal structure of an invertebrate cytolysin pore reveals unique properties and mechanism of assembly.

@article{Podobnik2016CrystalSO,
  title={Crystal structure of an invertebrate cytolysin pore reveals unique properties and mechanism of assembly.},
  author={Marjetka Podobnik and Peter Savory and Nejc Rojko and Matic Kisovec and Neil Wood and Richard Hambley and Jonathan Pugh and Elijah J Wallace and Luke A. McNeill and Mark Bruce and Idlir Liko and Timothy M. Allison and Shahid Mehmood and Neval Yilmaz and Toshihide Kobayashi and Robert J C Gilbert and Carol V Robinson and Lakmal Jayasinghe and Gregor Anderluh},
  journal={Nature communications},
  year={2016},
  volume={7},
  pages={11598}
}
The invertebrate cytolysin lysenin is a member of the aerolysin family of pore-forming toxins that includes many representatives from pathogenic bacteria. Here we report the crystal structure of the lysenin pore and provide insights into its assembly mechanism. The lysenin pore is assembled from nine monomers via dramatic reorganization of almost half of… CONTINUE READING