Structure and evolution of the Ivy protein family, unexpected lysozyme inhibitors in Gram-negative bacteria.

@article{Abergel2007StructureAE,
  title={Structure and evolution of the Ivy protein family, unexpected lysozyme inhibitors in Gram-negative bacteria.},
  author={Chantal Abergel and Vincent Monchois and Deborah Byrne and Sabine Chenivesse and Fr{\'e}d{\'e}rique Lembo and J C Lazzaroni and Jean-Michel Claverie},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2007},
  volume={104 15},
  pages={6394-9}
}
Part of an ancestral bactericidal system, vertebrate C-type lysozyme targets the peptidoglycan moiety of bacterial cell walls. We report the crystal structure of a protein inhibitor of C-type lysozyme, the Escherichia coli Ivy protein, alone and in complex with hen egg white lysozyme. Ivy exhibits a novel fold in which a protruding five-residue loop appears essential to its inhibitory effect. This feature guided the identification of Ivy orthologues in other Gram-negative bacteria. The… CONTINUE READING

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