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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Dates
Type | When |
---|---|
Created | 18 years, 10 months ago (Oct. 27, 2006, 2:19 p.m.) |
Deposited | 1 year, 7 months ago (Jan. 14, 2024, 11:45 p.m.) |
Indexed | 2 weeks, 1 day ago (Aug. 12, 2025, 6:04 p.m.) |
Issued | 30 years, 2 months ago (June 9, 1995) |
Published | 30 years, 2 months ago (June 9, 1995) |
Published Print | 30 years, 2 months ago (June 9, 1995) |
@article{Str_ter_1995, title={Crystal Structure of a Purple Acid Phosphatase Containing a Dinuclear Fe(III)-Zn(II) Active Site}, volume={268}, ISSN={1095-9203}, url={http://dx.doi.org/10.1126/science.7770774}, DOI={10.1126/science.7770774}, number={5216}, journal={Science}, publisher={American Association for the Advancement of Science (AAAS)}, author={Sträter, Norbert and Klabunde, Thomas and Tucker, Paul and Witzel, Herbert and Krebs, Bernt}, year={1995}, month=jun, pages={1489–1492} }