1t3k
From Proteopedia
(New page: 200px<br /><applet load="1t3k" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t3k" /> '''NMR structure of a CDC25-like dual-specifici...) |
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| - | [[Image:1t3k.jpg|left|200px]]<br /><applet load="1t3k" size=" | + | [[Image:1t3k.jpg|left|200px]]<br /><applet load="1t3k" size="350" color="white" frame="true" align="right" spinBox="true" |
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'''NMR structure of a CDC25-like dual-specificity tyrosine phosphatase of Arabidopsis thaliana'''<br /> | '''NMR structure of a CDC25-like dual-specificity tyrosine phosphatase of Arabidopsis thaliana'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The dual-specificity CDC25 phosphatases are critical positive regulators | + | The dual-specificity CDC25 phosphatases are critical positive regulators of cyclin-dependent kinases (CDKs). Even though an antagonistic Arabidopsis thaliana WEE1 kinase has been cloned and tyrosine phosphorylation of its CDKs has been demonstrated, no valid candidate for a CDC25 protein has been reported in higher plants. We identify a CDC25-related protein (Arath;CDC25) of A. thaliana, constituted by a sole catalytic domain. The protein has a tyrosine-phosphatase activity and stimulates the kinase activity of Arabidopsis CDKs. Its tertiary structure was obtained by NMR spectroscopy and confirms that Arath;CDC25 belongs structurally to the classical CDC25 superfamily with a central five-stranded beta-sheet surrounded by helices. A particular feature of the protein, however, is the presence of an additional zinc-binding loop in the C-terminal part. NMR mapping studies revealed the interaction with phosphorylated peptidic models derived from the conserved CDK loop containing the phosphothreonine-14 and phosphotyrosine-15. We conclude that despite sequence divergence, Arath;CDC25 is structurally and functionally an isoform of the CDC25 superfamily, which is conserved in yeast and in plants, including Arabidopsis and rice. |
==About this Structure== | ==About this Structure== | ||
| - | 1T3K is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], 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:// | + | 1T3K is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1T3K OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein-tyrosine-phosphatase]] | [[Category: Protein-tyrosine-phosphatase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Costa, M | + | [[Category: Costa, M da.]] |
[[Category: Dewitte, F.]] | [[Category: Dewitte, F.]] | ||
| - | [[Category: Faure, J | + | [[Category: Faure, J D.]] |
[[Category: Hassan, S.]] | [[Category: Hassan, S.]] | ||
[[Category: Inze, D.]] | [[Category: Inze, D.]] | ||
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[[Category: Lippens, G.]] | [[Category: Lippens, G.]] | ||
[[Category: Vandepoele, K.]] | [[Category: Vandepoele, K.]] | ||
| - | [[Category: Veylder, L | + | [[Category: Veylder, L De.]] |
| - | [[Category: Wieruszeski, J | + | [[Category: Wieruszeski, J M.]] |
[[Category: ZN]] | [[Category: ZN]] | ||
[[Category: cdc25]] | [[Category: cdc25]] | ||
| Line 30: | Line 30: | ||
[[Category: plant]] | [[Category: plant]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:09:30 2008'' |
Revision as of 13:09, 21 February 2008
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NMR structure of a CDC25-like dual-specificity tyrosine phosphatase of Arabidopsis thaliana
Overview
The dual-specificity CDC25 phosphatases are critical positive regulators of cyclin-dependent kinases (CDKs). Even though an antagonistic Arabidopsis thaliana WEE1 kinase has been cloned and tyrosine phosphorylation of its CDKs has been demonstrated, no valid candidate for a CDC25 protein has been reported in higher plants. We identify a CDC25-related protein (Arath;CDC25) of A. thaliana, constituted by a sole catalytic domain. The protein has a tyrosine-phosphatase activity and stimulates the kinase activity of Arabidopsis CDKs. Its tertiary structure was obtained by NMR spectroscopy and confirms that Arath;CDC25 belongs structurally to the classical CDC25 superfamily with a central five-stranded beta-sheet surrounded by helices. A particular feature of the protein, however, is the presence of an additional zinc-binding loop in the C-terminal part. NMR mapping studies revealed the interaction with phosphorylated peptidic models derived from the conserved CDK loop containing the phosphothreonine-14 and phosphotyrosine-15. We conclude that despite sequence divergence, Arath;CDC25 is structurally and functionally an isoform of the CDC25 superfamily, which is conserved in yeast and in plants, including Arabidopsis and rice.
About this Structure
1T3K is a Single protein structure of sequence from Arabidopsis thaliana with as ligand. Active as Protein-tyrosine-phosphatase, with EC number 3.1.3.48 Full crystallographic information is available from OCA.
Reference
A small CDC25 dual-specificity tyrosine-phosphatase isoform in Arabidopsis thaliana., Landrieu I, da Costa M, De Veylder L, Dewitte F, Vandepoele K, Hassan S, Wieruszeski JM, Corellou F, Faure JD, Van Montagu M, Inze D, Lippens G, Proc Natl Acad Sci U S A. 2004 Sep 7;101(36):13380-5. Epub 2004 Aug 25. PMID:15329414
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