Crystal structure of a purple acid phosphatase containing a dinuclear Fe(III)-Zn(II) active site.

@article{Strter1995CrystalSO,
  title={Crystal structure of a purple acid phosphatase containing a dinuclear Fe(III)-Zn(II) active site.},
  author={Norbert Str{\"a}ter and Thomas Klabunde and Philip T Tucker and Herbert Witzel and Bernt Krebs},
  journal={Science},
  year={1995},
  volume={268 5216},
  pages={1489-92}
}
Kidney bean purple acid phosphatase (KBPAP) is an Fe(III)-Zn(II) metalloenzyme resembling the mammalian Fe(III)-Fe(II) purple acid phosphatases. The structure of the homodimeric 111-kilodalton KBPAP was determined at a resolution of 2.9 angstroms. The enzyme contains two domains in each subunit. The active site is located in the carboxyl-terminal domain at… CONTINUE READING