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|1c25, resolution 2.30Å ()|
|Gene:||CDC25A (Homo sapiens)|
HUMAN CDC25A CATALYTIC DOMAIN
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.
Crystal structure of the catalytic domain of the human cell cycle control phosphatase, Cdc25A., Fauman EB, Cogswell JP, Lovejoy B, Rocque WJ, Holmes W, Montana VG, Piwnica-Worms H, Rink MJ, Saper MA, Cell. 1998 May 15;93(4):617-25. PMID:9604936
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
- Fauman EB, Cogswell JP, Lovejoy B, Rocque WJ, Holmes W, Montana VG, Piwnica-Worms H, Rink MJ, Saper MA. Crystal structure of the catalytic domain of the human cell cycle control phosphatase, Cdc25A. Cell. 1998 May 15;93(4):617-25. PMID:9604936
- Sandelin E. On hydrophobicity and conformational specificity in proteins. Biophys J. 2004 Jan;86(1 Pt 1):23-30. PMID:14695246 doi:10.1016/S0006-3495(04)74080-1
- Willis MS, Hogan JK, Prabhakar P, Liu X, Tsai K, Wei Y, Fox T. Investigation of protein refolding using a fractional factorial screen: a study of reagent effects and interactions. Protein Sci. 2005 Jul;14(7):1818-26. Epub 2005 Jun 3. PMID:15937284 doi:10.1110/ps.051433205