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Structure of alkaline phosphatases.

E E Kim1, H W Wyckoff

  • 1Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511.

Clinica Chimica Acta; International Journal of Clinical Chemistry
|January 15, 1990
PubMed
Summary
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The crystal structure of E. coli alkaline phosphatase (AP) was refined, revealing active site changes. This structure models mammalian APs, showing conserved active sites despite differences in size and association.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Alkaline phosphatase (AP) from Escherichia coli serves as a model for mammalian APs.
  • Understanding AP structure is crucial for elucidating enzyme function.

Purpose of the Study:

  • To refine the crystal structure of E. coli alkaline phosphatase (AP).
  • To model the three-dimensional structures of mammalian alkaline phosphatases based on the refined E. coli AP structure.

Main Methods:

  • X-ray crystallography to determine the crystal structure of E. coli AP.
  • Refinement of the crystal structure to a resolution of 2.0 Å.
  • Comparative sequence analysis and homology modeling to predict mammalian AP structures.

Main Results:

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  • The crystal structure of E. coli AP was refined to an R-factor of 0.184 at 2.0 Å resolution.
  • Significant changes were identified in the active site during refinement, including residue retracing and shifting.
  • The core structures of mammalian alkaline phosphatases were modeled, showing high homology to E. coli AP.

Conclusions:

  • The refined E. coli AP structure provides a basis for understanding mammalian AP structures.
  • Despite differences (size, glycosylation, membrane association), the active site of alkaline phosphatases is highly conserved.
  • Specific variations in ligands binding to phosphate and Mg ions were observed in the active site.