Structural snapshots of Escherichia coli histidinol phosphate phosphatase along the reaction pathway.

@article{Rangarajan2006StructuralSO,
  title={Structural snapshots of Escherichia coli histidinol phosphate phosphatase along the reaction pathway.},
  author={Erumbi S. Rangarajan and Ariane Proteau and John J. Wagner and Ming-ni Hung and Allan Matte and Miroslaw Cygler},
  journal={The Journal of biological chemistry},
  year={2006},
  volume={281 49},
  pages={37930-41}
}
HisB from Escherichia coli is a bifunctional enzyme catalyzing the sixth and eighth steps of l-histidine biosynthesis. The N-terminal domain (HisB-N) possesses histidinol phosphate phosphatase activity, and its crystal structure shows a single domain with fold similarity to the haloacid dehalogenase (HAD) enzyme family. HisB-N forms dimers in the crystal and in solution. The structure shows the presence of a structural Zn(2+) ion stabilizing the conformation of an extended loop. Two metal… CONTINUE READING

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