1C25

HUMAN CDC25A CATALYTIC DOMAIN

Summary for 1C25

• Entry DOI: 10.2210/pdb1c25/pdb
• Descriptor: CDC25A (2 entities in total)
• Functional Keywords: hydrolase, cell cycle phosphatase, dual specificity protein phosphatase, cdk2
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 19010.98

Authors

Fauman, E.B.,Cogswell, J.P.,Lovejoy, B.,Rocque, W.J.,Holmes, W.,Montana, V.G.,Piwnica-Worms, H.,Rink, M.J.,Saper, M.A. (deposition date: 1998-04-17, release date: 1998-08-19, Last modification date: 2024-02-07)

Primary citation

Fauman, E.B.,Cogswell, J.P.,Lovejoy, B.,Rocque, W.J.,Holmes, W.,Montana, V.G.,Piwnica-Worms, H.,Rink, M.J.,Saper, M.A.
Crystal structure of the catalytic domain of the human cell cycle control phosphatase, Cdc25A.
Cell(Cambridge,Mass.), 93:617-625, 1998

PubMed 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.

PubMed: 9604936
DOI: 10.1016/S0092-8674(00)81190-3

Experimental method

X-RAY DIFFRACTION (2.3 Å)