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| | ==NMR structure of a CDC25-like dual-specificity tyrosine phosphatase of Arabidopsis thaliana== | | ==NMR structure of a CDC25-like dual-specificity tyrosine phosphatase of Arabidopsis thaliana== |
| - | <StructureSection load='1t3k' size='340' side='right'caption='[[1t3k]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='1t3k' size='340' side='right'caption='[[1t3k]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1t3k]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T3K OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1T3K FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1t3k]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T3K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T3K FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CDC25 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1t3k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t3k OCA], [https://pdbe.org/1t3k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t3k RCSB], [https://www.ebi.ac.uk/pdbsum/1t3k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t3k ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1t3k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t3k OCA], [http://pdbe.org/1t3k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1t3k RCSB], [http://www.ebi.ac.uk/pdbsum/1t3k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1t3k ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CDC25_ARATH CDC25_ARATH]] Tyrosine protein phosphatase that dephosphorylates CDK complex and activate its kinase activity in vitro.<ref>PMID:16567632</ref> <ref>PMID:15329414</ref> Arsenate reductase that plays a major role in the reduction of arsenate to arsenite and arsenic retention in roots.<ref>PMID:16567632</ref> <ref>PMID:15329414</ref> | + | [https://www.uniprot.org/uniprot/CDC25_ARATH CDC25_ARATH] Tyrosine protein phosphatase that dephosphorylates CDK complex and activate its kinase activity in vitro.<ref>PMID:16567632</ref> <ref>PMID:15329414</ref> Arsenate reductase that plays a major role in the reduction of arsenate to arsenite and arsenic retention in roots.<ref>PMID:16567632</ref> <ref>PMID:15329414</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| | *[[Dual specificity phosphatase 3D structures|Dual specificity phosphatase 3D structures]] | | *[[Dual specificity phosphatase 3D structures|Dual specificity phosphatase 3D structures]] |
| - | *[[MAP kinase phosphatase|MAP kinase phosphatase]] | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Arath]] | + | [[Category: Arabidopsis thaliana]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Protein-tyrosine-phosphatase]] | + | [[Category: De Veylder L]] |
| - | [[Category: Costa, M da]]
| + | [[Category: Dewitte F]] |
| - | [[Category: Dewitte, F]] | + | [[Category: Faure JD]] |
| - | [[Category: Faure, J D]] | + | [[Category: Hassan S]] |
| - | [[Category: Hassan, S]] | + | [[Category: Inze D]] |
| - | [[Category: Inze, D]] | + | [[Category: Landrieu I]] |
| - | [[Category: Landrieu, I]] | + | [[Category: Lippens G]] |
| - | [[Category: Lippens, G]] | + | [[Category: Vandepoele K]] |
| - | [[Category: Vandepoele, K]] | + | [[Category: Wieruszeski JM]] |
| - | [[Category: Veylder, L De]] | + | [[Category: Da Costa M]] |
| - | [[Category: Wieruszeski, J M]] | + | |
| - | [[Category: Cdc25]]
| + | |
| - | [[Category: Cell cycle]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Phosphorylation]]
| + | |
| - | [[Category: Plant]]
| + | |
| Structural highlights
Function
CDC25_ARATH Tyrosine protein phosphatase that dephosphorylates CDK complex and activate its kinase activity in vitro.[1] [2] Arsenate reductase that plays a major role in the reduction of arsenate to arsenite and arsenic retention in roots.[3] [4]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Dhankher OP, Rosen BP, McKinney EC, Meagher RB. Hyperaccumulation of arsenic in the shoots of Arabidopsis silenced for arsenate reductase (ACR2). Proc Natl Acad Sci U S A. 2006 Apr 4;103(14):5413-8. Epub 2006 Mar 27. PMID:16567632 doi:http://dx.doi.org/10.1073/pnas.0509770102
- ↑ 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. A small CDC25 dual-specificity tyrosine-phosphatase isoform in Arabidopsis thaliana. Proc Natl Acad Sci U S A. 2004 Sep 7;101(36):13380-5. Epub 2004 Aug 25. PMID:15329414 doi:10.1073/pnas.0405248101
- ↑ Dhankher OP, Rosen BP, McKinney EC, Meagher RB. Hyperaccumulation of arsenic in the shoots of Arabidopsis silenced for arsenate reductase (ACR2). Proc Natl Acad Sci U S A. 2006 Apr 4;103(14):5413-8. Epub 2006 Mar 27. PMID:16567632 doi:http://dx.doi.org/10.1073/pnas.0509770102
- ↑ 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. A small CDC25 dual-specificity tyrosine-phosphatase isoform in Arabidopsis thaliana. Proc Natl Acad Sci U S A. 2004 Sep 7;101(36):13380-5. Epub 2004 Aug 25. PMID:15329414 doi:10.1073/pnas.0405248101
- ↑ 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. A small CDC25 dual-specificity tyrosine-phosphatase isoform in Arabidopsis thaliana. Proc Natl Acad Sci U S A. 2004 Sep 7;101(36):13380-5. Epub 2004 Aug 25. PMID:15329414 doi:10.1073/pnas.0405248101
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