PMID:9604936

Citation	Fauman, EB, Cogswell, JP, Lovejoy, B, Rocque, WJ, Holmes, W, Montana, VG, Piwnica-Worms, H, Rink, MJ and Saper, MA (1998) Crystal structure of the catalytic domain of the human cell cycle control phosphatase, Cdc25A. Cell 93:617-25
Abstract	Cdc25 phosphatases activate the cell division kinases throughout the cell cycle. The 2.3 A structure of the human Cdc25A catalytic domain reveals a small alpha/beta domain with a fold unlike previously described phosphatase structures but identical to rhodanese, a sulfur-transfer protein. Only the active-site loop, containing the Cys-(X)5-Arg motif, shows similarity to the tyrosine phosphatases. In some crystals, the catalytic Cys-430 forms a disulfide bond with the invariant Cys-384, suggesting that Cdc25 may be self-inhibited during oxidative stress. Asp-383, previously proposed to be the general acid, instead serves a structural role, forming a conserved buried salt-bridge. We propose that Glu-431 may act as a general acid. Structure-based alignments suggest that the noncatalytic domain of the MAP kinase phosphatases will share this topology, as will ACR2, a eukaryotic arsenical resistance protein.
Links	PubMed
Keywords	Amino Acid Sequence; Binding Sites; Crystallography, X-Ray; Disulfides/chemistry; Humans; Models, Molecular; Molecular Sequence Data; Protein Conformation; Protein Tyrosine Phosphatases/chemistry; Sequence Alignment; Substrate Specificity; cdc25 Phosphatases
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