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A complex iron-calcium cofactor catalyzing phosphotransfer chemistry.

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Microbial alkaline phosphatases like PhoX use a complex iron-cofactor for phosphate acquisition. This structure reveals how the enzyme binds substrates, suggesting iron availability may limit microbial phosphate uptake.

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Area of Science:

  • Biochemistry
  • Microbiology
  • Enzymology

Background:

  • Alkaline phosphatases are vital for microorganisms to acquire phosphate.
  • Understanding the catalytic mechanisms of these enzymes is crucial.

Purpose of the Study:

  • To determine the structure of the microbial alkaline phosphatase PhoX.
  • To elucidate the catalytic mechanism and active-site cofactor of PhoX.

Main Methods:

  • X-ray crystallography was used to determine the structure of PhoX.
  • Structures of PhoX-ligand complexes were analyzed.

Main Results:

  • The PhoX active site contains a unique cofactor with two ferric iron ions, three calcium ions, and an oxo group.
  • The cofactor structure resembles synthetic oxide-centered triangular metal complexes.
  • Substrate binding involves active-site metal ions, and the oxo group is implicated in catalysis.

Conclusions:

  • The determined structure provides insights into PhoX enzymatic activity.
  • The presence of iron in the cofactor suggests iron bioavailability could limit microbial phosphate acquisition.