The crystal structures of EAP domains from Staphylococcus aureus reveal an unexpected homology to bacterial superantigens.

@article{Geisbrecht2005TheCS,
  title={The crystal structures of EAP domains from Staphylococcus aureus reveal an unexpected homology to bacterial superantigens.},
  author={Brian V. Geisbrecht and Brent Y. Hamaoka and Benjamin Perman and Adam Zemla and Daniel J. Leahy},
  journal={The Journal of biological chemistry},
  year={2005},
  volume={280 17},
  pages={17243-50}
}
The Eap (extracellular adherence protein) of Staphylococcus aureus functions as a secreted virulence factor by mediating interactions between the bacterial cell surface and several extracellular host proteins. Eap proteins from different Staphylococcal strains consist of four to six tandem repeats of a structurally uncharacterized domain (EAP domain). We have determined the three-dimensional structures of three different EAP domains to 1.8, 2.2, and 1.35 A resolution, respectively. These… CONTINUE READING

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