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==NMR structure of a CDC25-like dual-specificity tyrosine phosphatase of Arabidopsis thaliana== | |||
<StructureSection load='1t3k' size='340' side='right'caption='[[1t3k]]' scene=''> | |||
== Structural highlights == | |||
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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='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> | |||
== Function == | |||
[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 == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/t3/1t3k_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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="background-color:#fffaf0;"> | |||
== 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<ref>PMID:15329414</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1t3k" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[ | *[[Dual specificity phosphatase 3D structures|Dual specificity phosphatase 3D structures]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Arabidopsis thaliana]] | [[Category: Arabidopsis thaliana]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: De Veylder L]] | ||
[[Category: Dewitte | [[Category: Dewitte F]] | ||
[[Category: Faure | [[Category: Faure JD]] | ||
[[Category: Hassan | [[Category: Hassan S]] | ||
[[Category: Inze | [[Category: Inze D]] | ||
[[Category: Landrieu | [[Category: Landrieu I]] | ||
[[Category: Lippens | [[Category: Lippens G]] | ||
[[Category: Vandepoele | [[Category: Vandepoele K]] | ||
[[Category: | [[Category: Wieruszeski JM]] | ||
[[Category: | [[Category: Da Costa M]] | ||
Latest revision as of 12:11, 22 May 2024
NMR structure of a CDC25-like dual-specificity tyrosine phosphatase of Arabidopsis thalianaNMR structure of a CDC25-like dual-specificity tyrosine phosphatase of Arabidopsis thaliana
Structural highlights
FunctionCDC25_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 PubMedThe 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 AlsoReferences
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