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==Crystal structure of dual specificity protein phosphatase 23 from Homo sapiens in complex with ligand malate ion== | ==Crystal structure of dual specificity protein phosphatase 23 from Homo sapiens in complex with ligand malate ion== | ||
<StructureSection load='2img' size='340' side='right' caption='[[2img]], [[Resolution|resolution]] 1.93Å' scene=''> | <StructureSection load='2img' size='340' side='right'caption='[[2img]], [[Resolution|resolution]] 1.93Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'> | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IMG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IMG FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.93Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MLT:D-MALATE'>MLT</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=2img FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2img OCA], [https://pdbe.org/2img PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2img RCSB], [https://www.ebi.ac.uk/pdbsum/2img PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2img ProSAT], [https://www.topsan.org/Proteins/NYSGXRC/2img TOPSAN]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/im/2img_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/im/2img_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
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</div> | </div> | ||
<div class="pdbe-citations 2img" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 2img" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[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: | [[Category: Large Structures]] | ||
[[Category: Agarwal | [[Category: Agarwal R]] | ||
[[Category: Burley | [[Category: Burley SK]] | ||
[[Category: Swaminathan S]] | |||
[[Category: Swaminathan | |||
Latest revision as of 11:13, 30 October 2024
Crystal structure of dual specificity protein phosphatase 23 from Homo sapiens in complex with ligand malate ionCrystal structure of dual specificity protein phosphatase 23 from Homo sapiens in complex with ligand malate ion
Structural highlights
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 PubMedProtein phosphorylation plays a crucial role in mitogenic signal transduction and regulation of cell growth and differentiation. Dual specificity protein phosphatase 23 (DUSP23) or VHZ mediates dephosphorylation of phospho-tyrosyl (pTyr) and phospho-seryl/threonyl (pSer/pThr) residues in specific proteins. In vitro, it can dephosphorylate p44ERK1 but not p54SAPK-beta and enhance activation of c-Jun N-terminal kinase (JNK) and p38. Human VHZ, the smallest of the catalytically active protein-tyrosine phosphatases (PTP) reported to date (150 residues), is a class I Cys-based PTP and bears the distinctive active site signature motif HCXXGXXRS(T). We present the crystal structure of VHZ determined at 1.93A resolution. The polypeptide chain adopts the typical alphabetaalpha PTP fold, giving rise to a shallow active site cleft that supports dual phosphorylated substrate specificity. Within our crystals, the Thr-135-Tyr-136 from a symmetry-related molecule bind in the active site with a malate ion, where they mimic the phosphorylated TY motif of the MAPK activation loop in an enzyme-substrate/product complex. Analyses of intermolecular interactions between the enzyme and this pseudo substrate/product along with functional analysis of Phe-66, Leu-97, and Phe-99 residues provide insights into the mechanism of substrate binding and catalysis in VHZ. Structure of human dual specificity protein phosphatase 23, VHZ, enzyme-substrate/product complex.,Agarwal R, Burley SK, Swaminathan S J Biol Chem. 2008 Apr 4;283(14):8946-53. Epub 2008 Feb 1. PMID:18245086[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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