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The topology of the catalytic domain of Cdc25A, a cell cycle control phosphatase has been determined at a resolution of 2.3 angstrom units. The domain consists of an alpha/beta motif different from that of other phasphatases. However, it shares some similarity with a sulphur-transfer protein, rhodanese. The structural and functional roles of specific amino acid residues in this enzyme are presented.

Protein dephosphorylation is a chemical reaction involved in the regulation of physiological processes such as glycogen metabolism, signal transduction, and osmoregulation. There are two classes of enzymes that regulate protein dephosphorylation: protein kinases and protein phosphatases. The latter are further subdivided into two, metallo-protein phosphatases and protein tyrosine phosphatases. An overview of the structure and function of these enzymes is presented.