1t3k

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(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="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1t3k" />
 
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'''NMR structure of a CDC25-like dual-specificity tyrosine phosphatase of Arabidopsis thaliana'''<br />
 
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==Overview==
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==NMR structure of a CDC25-like dual-specificity tyrosine phosphatase of Arabidopsis thaliana==
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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.
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<StructureSection load='1t3k' size='340' side='right'caption='[[1t3k]]' scene=''>
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== Structural highlights ==
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<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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<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>
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<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>
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/t3/1t3k_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1t3k ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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<ref>PMID:15329414</ref>
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1T3K OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15329414 15329414]
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</div>
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[[Category: Arabidopsis thaliana]]
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<div class="pdbe-citations 1t3k" style="background-color:#fffaf0;"></div>
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[[Category: Protein-tyrosine-phosphatase]]
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[[Category: Single protein]]
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[[Category: Costa, M.da.]]
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[[Category: Dewitte, F.]]
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[[Category: Faure, J.D.]]
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[[Category: Hassan, S.]]
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[[Category: Inze, D.]]
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[[Category: Landrieu, I.]]
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[[Category: Lippens, G.]]
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[[Category: Vandepoele, K.]]
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[[Category: Veylder, L.De.]]
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[[Category: Wieruszeski, J.M.]]
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[[Category: ZN]]
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[[Category: cdc25]]
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[[Category: cell cycle]]
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[[Category: phosphorylation]]
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[[Category: plant]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:57:41 2007''
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==See Also==
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*[[Dual specificity phosphatase 3D structures|Dual specificity phosphatase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Arabidopsis thaliana]]
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[[Category: Large Structures]]
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[[Category: De Veylder L]]
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[[Category: Dewitte F]]
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[[Category: Faure JD]]
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[[Category: Hassan S]]
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[[Category: Inze D]]
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[[Category: Landrieu I]]
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[[Category: Lippens G]]
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[[Category: Vandepoele K]]
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[[Category: Wieruszeski JM]]
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[[Category: Da Costa M]]

Current revision

NMR structure of a CDC25-like dual-specificity tyrosine phosphatase of Arabidopsis thaliana

PDB ID 1t3k

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