3c5v

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[[Image:3c5v.jpg|left|200px]]
 
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==PP2A-specific methylesterase apo form (PME)==
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The line below this paragraph, containing "STRUCTURE_3c5v", creates the "Structure Box" on the page.
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<StructureSection load='3c5v' size='340' side='right'caption='[[3c5v]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3c5v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C5V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3C5V FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</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=3c5v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c5v OCA], [https://pdbe.org/3c5v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3c5v RCSB], [https://www.ebi.ac.uk/pdbsum/3c5v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3c5v ProSAT]</span></td></tr>
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{{STRUCTURE_3c5v| PDB=3c5v | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PPME1_HUMAN PPME1_HUMAN] Demethylates proteins that have been reversibly carboxymethylated. Demethylates PPP2CB (in vitro) and PPP2CA. Binding to PPP2CA displaces the manganese ion and inactivates the enzyme.<ref>PMID:10318862</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/c5/3c5v_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=3c5v ConSurf].
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<div style="clear:both"></div>
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'''PP2A-specific methylesterase apo form (PME)'''
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==See Also==
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*[[Methylesterase 3D structures|Methylesterase 3D structures]]
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== References ==
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==Overview==
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<references/>
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Protein phosphatase 2A (PP2A) is an important serine/threonine phosphatase that plays a role in many biological processes. Reversible carboxyl methylation of the PP2A catalytic subunit is an essential regulatory mechanism for its function. Demethylation and negative regulation of PP2A is mediated by a PP2A-specific methylesterase PME-1, which is conserved from yeast to humans. However, the underlying mechanism of PME-1 function remains enigmatic. Here we report the crystal structures of PME-1 by itself and in complex with a PP2A heterodimeric core enzyme. The structures reveal that PME-1 directly binds to the active site of PP2A and that this interaction results in the activation of PME-1 by rearranging the catalytic triad into an active conformation. Strikingly, these interactions also lead to inactivation of PP2A by evicting the manganese ions that are required for the phosphatase activity of PP2A. These observations identify a dual role of PME-1 that regulates PP2A activation, methylation, and holoenzyme assembly in cells.
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__TOC__
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</StructureSection>
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==About this Structure==
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3C5V is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C5V OCA].
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==Reference==
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Structural mechanism of demethylation and inactivation of protein phosphatase 2A., Xing Y, Li Z, Chen Y, Stock JB, Jeffrey PD, Shi Y, Cell. 2008 Apr 4;133(1):154-63. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18394995 18394995]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Chen, Y.]]
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[[Category: Chen Y]]
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[[Category: Jeffrey, P D.]]
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[[Category: Jeffrey PD]]
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[[Category: Li, Z.]]
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[[Category: Li Z]]
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[[Category: Shi, Y.]]
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[[Category: Shi Y]]
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[[Category: Stock, J.]]
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[[Category: Stock J]]
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[[Category: Xing, Y.]]
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[[Category: Xing Y]]
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[[Category: Alternative splicing]]
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[[Category: Demethylase]]
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[[Category: Hydrolase]]
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[[Category: Phosphoprotein]]
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[[Category: Pp2a]]
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[[Category: Serine esterase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 11 10:57:53 2008''
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Current revision

PP2A-specific methylesterase apo form (PME)

PDB ID 3c5v

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