1c25: Difference between revisions
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Revision as of 16:52, 5 November 2007
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HUMAN CDC25A CATALYTIC DOMAIN
OverviewOverview
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.
About this StructureAbout this Structure
1C25 is a Single protein structure of sequence from Homo sapiens. Active as Protein-tyrosine-phosphatase, with EC number 3.1.3.48 Structure known Active Sites: DSU and POP. Full crystallographic information is available from OCA.
ReferenceReference
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
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