Structures of trehalose-6-phosphate phosphatase from pathogenic fungi reveal the mechanisms of substrate recognition and catalysis.

@article{Miao2016StructuresOT,
  title={Structures of trehalose-6-phosphate phosphatase from pathogenic fungi reveal the mechanisms of substrate recognition and catalysis.},
  author={Yi Miao and Jennifer L. Tenor and Dena L. Toffaletti and Erica J Washington and Jiuyu Liu and William Robert Shadrick and Maria A. Schumacher and Richard E. Lee and John R Perfect and Richard G Brennan},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2016},
  volume={113 26},
  pages={7148-53}
}
Trehalose is a disaccharide essential for the survival and virulence of pathogenic fungi. The biosynthesis of trehalose requires trehalose-6-phosphate synthase, Tps1, and trehalose-6-phosphate phosphatase, Tps2. Here, we report the structures of the N-terminal domain of Tps2 (Tps2NTD) from Candida albicans, a transition-state complex of the Tps2 C-terminal trehalose-6-phosphate phosphatase domain (Tps2PD) bound to BeF3 and trehalose, and catalytically dead Tps2PD(D24N) from Cryptococcus… CONTINUE READING
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