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A Model of the Transition State in the Alkaline Phosphatase Reaction*

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A high resolution crystal structure ofEscherichia coli alkaline phosphatase in the presence of vanadate has been refined to 1.9 Å resolution. The vanadate ion takes on a trigonal bipyramidal geometry and is covalently bound by the active site serine nucleophile. A coordinated water molecule occupies the axial position opposite the serine nucleophile, whereas the equatorial oxygen atoms of the vanadate ion are stabilized by interactions with both Arg-166 and the zinc metal ions of the active site. This structural complex supports the in-line displacement mechanism of phosphomonoester hydrolysis by alkaline phosphatase and provides a model for the proposed transition state in the enzyme-catalyzed reaction.

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*

This work was supported by Grant GM42833 from the National Institutes of Health.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The atomic coordinates and structure factors (code 1B8J ) have been deposited in the Protein Data Bank, Brookhaven National Laboratory, Upton, NY.

‡

To whom all reprint requests should be addressed: Dept. of Chemistry, Merkert Chemistry Center, Boston College, Chestnut Hill, MA 02167.

© 1999 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.