Structures of open (R) and close (T) states of prephenate dehydratase (PDT)--implication of allosteric regulation by L-phenylalanine.

@article{Tan2008StructuresOO,
  title={Structures of open (R) and close (T) states of prephenate dehydratase (PDT)--implication of allosteric regulation by L-phenylalanine.},
  author={Kemin Tan and Hui Li and Rongguang Zhang and Minyi Gu and Shonda T Clancy and Andrzej Joachimiak},
  journal={Journal of structural biology},
  year={2008},
  volume={162 1},
  pages={94-107}
}
The enzyme prephenate dehydratase (PDT) converts prephenate to phenylpyruvate in L-phenylalanine biosynthesis. PDT is allosterically regulated by L-Phe and other amino acids. We report the first crystal structures of PDT from Staphylococcus aureus in a relaxed (R) state and PDT from Chlorobium tepidum in a tense (T) state. The two enzymes show low sequence identity (27.3%) but the same prototypic architecture and domain organization. Both enzymes are tetramers (dimer of dimers) in crystal and… CONTINUE READING