Structural basis for substrate recognition by a unique Legionella phosphoinositide phosphatase.

@article{Hsu2012StructuralBF,
  title={Structural basis for substrate recognition by a unique Legionella phosphoinositide phosphatase.},
  author={FoSheng Hsu and Wenhan Zhu and Lucy C Brennan and Lili Tao and Zhao-Qing Luo and Yuxin Mao},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2012},
  volume={109 34},
  pages={13567-72}
}
Legionella pneumophila is an opportunistic intracellular pathogen that causes sporadic and epidemic cases of Legionnaires' disease. Emerging data suggest that Legionella infection involves the subversion of host phosphoinositide (PI) metabolism. However, how this bacterium actively manipulates PI lipids to benefit its infection is still an enigma. Here, we report that the L. pneumophila virulence factor SidF is a phosphatidylinositol polyphosphate 3-phosphatase that specifically hydrolyzes the… CONTINUE READING

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