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Updated: Jul 21, 2026

Production, Crystallization and Structure Determination of C. difficile PPEP-1 via Microseeding and Zinc-SAD
Published on: December 30, 2016
Crystal structure of human prostatic acid phosphatase .
C G Jakob1, K Lewinski, R Kuciel
1Department of Chemistry and Biochemistry, University of South Carolina, Columbia, South Carolina 29208, USA.
The crystal structure of human prostatic acid phosphatase (hPAP) reveals conserved catalytic residues, similar to rat PAP. This structural similarity supports extending mechanistic studies of rat PAP to the human enzyme.
Area of Science:
- Biochemistry
- Structural Biology
- Enzymology
Background:
- Human prostatic acid phosphatase (hPAP) is a key prostate gland product.
- The physiological substrate for hPAP remains unidentified.
Purpose of the Study:
- To determine the crystal structure of human prostatic acid phosphatase (hPAP).
- To compare the structure of hPAP with other histidine phosphatases.
- To investigate the glycosylation patterns of hPAP.
Main Methods:
- Purification of hPAP from human semen.
- Crystallization using polyethylene glycol.
- X-ray diffraction for crystal structure determination.
- Structure refinement to 3.1 Å resolution.
Main Results:
- The 3D structure of hPAP is highly similar to other histidine phosphatases, with conserved catalytic residues.
- N-linked carbohydrates are attached at all potential glycosylation sites.
- Specific attachment sites for high-mannose and complex carbohydrate chains were identified.
Conclusions:
- The structural similarity between human and rat PAP supports extending mechanistic studies from rat to human enzyme.
- Crystallographic data enabled correlation of N-linked carbohydrate attachment sites with specific carbohydrate types.
- Differences in complex carbohydrate attachment were observed between hPAP produced in prostate cells versus a baculovirus system.
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