1T3K
NMR structure of a CDC25-like dual-specificity tyrosine phosphatase of Arabidopsis thaliana
Summary for 1T3K
| Entry DOI | 10.2210/pdb1t3k/pdb |
| Descriptor | Dual-specificity tyrosine phosphatase, ZINC ION (2 entities in total) |
| Functional Keywords | cdc25, cell cycle, phosphorylation, plant, hydrolase |
| Biological source | Arabidopsis thaliana (thale cress) |
| Cellular location | Nucleus (Probable): Q8GY31 |
| Total number of polymer chains | 1 |
| Total formula weight | 17006.63 |
| Authors | Landrieu, I.,da Costa, M.,De Veylder, L.,Dewitte, F.,Vandepoele, K.,Hassan, S.,Wieruszeski, J.M.,Faure, J.D.,Inze, D.,Lippens, G. (deposition date: 2004-04-27, release date: 2004-09-07, Last modification date: 2024-05-22) |
| Primary citation | Landrieu, I.,Da Costa, M.,De Veylder, L.,Dewitte, F.,Vandepoele, K.,Hassan, S.,Wieruszeski, J.M.,Faure, J.D.,Van Montagu, M.,Inze, D.,Lippens, G. A small CDC25 dual-specificity tyrosine-phosphatase isoform in Arabidopsis thaliana. Proc.Natl.Acad.Sci.Usa, 101:13380-13385, 2004 Cited by PubMed Abstract: 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. PubMed: 15329414DOI: 10.1073/pnas.0405248101 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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