1c25: Difference between revisions
New page: left|200px<br /> <applet load="1c25" size="450" color="white" frame="true" align="right" spinBox="true" caption="1c25, resolution 2.3Å" /> '''HUMAN CDC25A CATALYT... |
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==About this Structure== | ==About this Structure== | ||
1C25 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1C25 OCA]]. | 1C25 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]]. Active as [[http://en.wikipedia.org/wiki/Hydrolase Hydrolase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48]]. Structure known Active Sites: DSU and POP. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1C25 OCA]]. | ||
==Reference== | ==Reference== | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
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Revision as of 09:42, 30 October 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 ... [(full description)]
About this StructureAbout this Structure
1C25 is a [Single protein] structure of sequence from [Homo sapiens]. Active as [Hydrolase], 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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