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Science 9 June 1995:
Vol. 268. no. 5216, pp. 1489 - 1492
DOI: 10.1126/science.7770774
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Articles

Science, Vol 268, Issue 5216, 1489-1492
Copyright © 1995 by American Association for the Advancement of Science

articles

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

N Strater, T Klabunde, P Tucker, H Witzel, and B Krebs

Anorganisch-Chemisches Institut, Universitat Munster, Germany.

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 the carboxy end of two sandwiched beta alpha beta alpha beta motifs. The two metal ions are 3.1 angstroms apart and bridged monodentately by Asp164. The iron is further coordinated by Tyr167, His325, and Asp135, and the zinc by His286, His323, and Asn201. The active-site structure is consistent with previous proposals regarding the mechanism of phosphate ester hydrolysis involving nucleophilic attack on the phosphate group by an Fe(III)-coordinated hydroxide ion.


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