1t3k

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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==
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<StructureSection load='1t3k' size='340' side='right'caption='[[1t3k]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<StructureSection load='1t3k' size='340' side='right'caption='[[1t3k]]' scene=''>
== Structural highlights ==
== 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/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 [https://proteopedia.org/fgij/fg.htm?mol=1T3K FirstGlance]. <br>
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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='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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</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CDC25 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] </span></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>
<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>
</table>
</table>
== Function ==
== 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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[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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</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].
</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].
<div style="clear:both"></div>
<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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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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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1t3k" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Arath]]
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[[Category: Arabidopsis thaliana]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Protein-tyrosine-phosphatase]]
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[[Category: De Veylder L]]
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[[Category: Costa, M da]]
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[[Category: Dewitte F]]
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[[Category: Dewitte, F]]
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[[Category: Faure JD]]
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[[Category: Faure, J D]]
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[[Category: Hassan S]]
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[[Category: Hassan, S]]
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[[Category: Inze D]]
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[[Category: Inze, D]]
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[[Category: Landrieu I]]
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[[Category: Landrieu, I]]
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[[Category: Lippens G]]
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[[Category: Lippens, G]]
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[[Category: Vandepoele K]]
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[[Category: Vandepoele, K]]
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[[Category: Wieruszeski JM]]
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[[Category: Veylder, L De]]
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[[Category: Da Costa M]]
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[[Category: Wieruszeski, J M]]
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[[Category: Cdc25]]
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[[Category: Cell cycle]]
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[[Category: Hydrolase]]
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[[Category: Phosphorylation]]
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[[Category: Plant]]
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Revision as of 08:37, 1 May 2024

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

PDB ID 1t3k

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