Structure of the Shigella T3SS effector IpaH defines a new class of E3 ubiquitin ligases

@article{Singer2008StructureOT,
  title={Structure of the Shigella T3SS effector IpaH defines a new class of E3 ubiquitin ligases},
  author={A. Singer and J. Rohde and R. Lam and T. Skarina and O. Kagan and Rosa DiLeo and N. Chirgadze and M. Cuff and A. Joachimiak and M. Tyers and P. Sansonetti and C. Parsot and A. Savchenko},
  journal={Nature Structural &Molecular Biology},
  year={2008},
  volume={15},
  pages={1293-1301}
}
  • A. Singer, J. Rohde, +10 authors A. Savchenko
  • Published 2008
  • Biology, Medicine
  • Nature Structural &Molecular Biology
  • IpaH proteins are E3 ubiquitin ligases delivered by the type III secretion apparatus into host cells upon infection of humans by the Gram-negative pathogen Shigella flexneri. These proteins comprise a variable leucine-rich repeat–containing N-terminal domain and a conserved C-terminal domain harboring an invariant cysteine residue that is crucial for activity. IpaH homologs are encoded by diverse animal and plant pathogens. Here we demonstrate that the IpaH C-terminal domain carries the… CONTINUE READING
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