1c25: Difference between revisions
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==Overview== | ==Overview== | ||
Cdc25 phosphatases activate the cell division kinases throughout the cell | 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 Structure== | ==About this Structure== | ||
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[[Category: Protein-tyrosine-phosphatase]] | [[Category: Protein-tyrosine-phosphatase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Cogswell, J | [[Category: Cogswell, J P.]] | ||
[[Category: Fauman, E | [[Category: Fauman, E B.]] | ||
[[Category: Holmes, W.]] | [[Category: Holmes, W.]] | ||
[[Category: Lovejoy, B.]] | [[Category: Lovejoy, B.]] | ||
[[Category: Montana, V | [[Category: Montana, V G.]] | ||
[[Category: Piwnica-Worms, H.]] | [[Category: Piwnica-Worms, H.]] | ||
[[Category: Rink, M | [[Category: Rink, M J.]] | ||
[[Category: Rocque, W | [[Category: Rocque, W J.]] | ||
[[Category: Saper, M | [[Category: Saper, M A.]] | ||
[[Category: cdk2]] | [[Category: cdk2]] | ||
[[Category: cell cycle phosphatase]] | [[Category: cell cycle phosphatase]] | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:01:35 2008'' | ||
Revision as of 13:01, 21 February 2008
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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 Known structural/functional Sites: and . 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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