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Crystal Structure of a Purple Acid Phosphatase Containing a Dinuclear Fe(III)-Zn(II) Active Site

Sträter, Norbert, Klabunde, Thomas, Tucker, Paul, Witzel, Herbert, Krebs, Bernt·1995·Science

Abstract

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 βαβαβ motifs. The two metal ions are 3.1 angstroms apart and bridged monodentately by Asp 164 . The iron is further coordinated by Tyr 167 , His 325 , and Asp 135 , and the zinc by His 286 , His 323 , and Asn 201 . 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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Metadata

Authors
Sträter, N., Klabunde, T., Tucker, P., Witzel, H., & Krebs, B.
Venue
Science
Published
1995-06-09
Volume
268
Issue
5216
Pages
1489-1492
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2020386376
Cited by
434
References
0
FWCI
34.74
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Crystal Structure of a Purple Acid Phosphatase Containing a Dinuclear Fe(III)-Zn(II) Active Site. https://app.cochat.ai/papers/10.1126/science.7770774
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Sträter, N., Klabunde, T., Tucker, P., Witzel, H., & Krebs, B. (1995). Crystal Structure of a Purple Acid Phosphatase Containing a Dinuclear Fe(III)-Zn(II) Active Site. Science. https://doi.org/10.1126/science.7770774

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