1c25: Difference between revisions

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[[Image:1c25.gif|left|200px]]
{{Seed}}
[[Image:1c25.png|left|200px]]


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{{STRUCTURE_1c25|  PDB=1c25  |  SCENE=  }}  
{{STRUCTURE_1c25|  PDB=1c25  |  SCENE=  }}  


'''HUMAN CDC25A CATALYTIC DOMAIN'''
===HUMAN CDC25A CATALYTIC DOMAIN===




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_9604936}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 9604936 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9604936}}


==About this Structure==
==About this Structure==
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[[Category: Cell cycle phosphatase,dual specificity protein phosphatase]]
[[Category: Cell cycle phosphatase,dual specificity protein phosphatase]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
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