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Three-dimensional structure of rat acid phosphatase
G Schneider1, Y Lindqvist, P Vihko
1Department of Molecular Biology, Swedish University of Agricultural Sciences, Uppsala Biomedical Center.
The EMBO Journal
|July 1, 1993
Summary
The crystal structure of rat prostatic acid phosphatase was determined, revealing a two-domain enzyme. This structure provides insights into enzyme function and potential therapeutic targets.
Area of Science:
- Biochemistry
- Structural Biology
- Enzymology
Background:
- Recombinant rat prostatic acid phosphatase (PAP) is an enzyme with significant biological roles.
- Understanding its three-dimensional structure is crucial for elucidating its function and developing targeted therapies.
Purpose of the Study:
- To determine the high-resolution crystal structure of recombinant rat prostatic acid phosphatase.
- To correlate the structural findings with the enzyme's biochemical properties and mutagenesis data.
Main Methods:
- Protein crystallography was employed to determine the crystal structure.
- The structure was resolved to 3 Angstrom resolution.
Main Results:
- The enzyme subunit comprises an alpha/beta domain and a smaller alpha domain.
- Two disulfide bridges (residues 129-340 and 315-319) and glycosylation sites were identified.
- Dimer formation extends the beta-sheet to 14 strands, with the active site located at the carboxy end of the alpha/beta domain.
- A chloride ion was observed at the phosphate binding site.
Conclusions:
- The determined three-dimensional structure of rat prostatic acid phosphatase offers a detailed molecular model.
- Structural insights can guide future studies on enzyme mechanisms and inhibitor design.
- The findings provide a basis for correlating structure with biochemical activity and mutagenesis results.