Crystal structure of the functional region of Uro-adherence factor A from Staphylococcus saprophyticus reveals participation of the B domain in ligand binding.

@article{Matsuoka2011CrystalSO,
  title={Crystal structure of the functional region of Uro-adherence factor A from Staphylococcus saprophyticus reveals participation of the B domain in ligand binding.},
  author={Eriko Matsuoka and Yoshikazu Tanaka and Makoto Kuroda and Yuko Shouji and Toshiko Ohta and Isao Tanaka and Min Li Yao},
  journal={Protein science : a publication of the Protein Society},
  year={2011},
  volume={20 2},
  pages={406-16}
}
Staphylococci use cell wall-anchored proteins as adhesins to attach to host tissues. Staphylococcus saprophyticus, a uropathogenic species, has a unique cell wall-anchored protein, uro-adherence factor A (UafA), which shows erythrocyte binding activity. To investigate the mechanism of adhesion by UafA, we determined the crystal structure of the functional region of UafA at 1.5 Å resolution. The structure was composed of three domains, designated as the N2, N3, and B domains, arranged in a… CONTINUE READING