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4i5j

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==PP2A PR70 Holoenzyme==
==PP2A PR70 Holoenzyme==
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<StructureSection load='4i5j' size='340' side='right' caption='[[4i5j]], [[Resolution|resolution]] 2.09&Aring;' scene=''>
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<StructureSection load='4i5j' size='340' side='right'caption='[[4i5j]], [[Resolution|resolution]] 2.09&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4i5j]] is a 1 chain structure with 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=4I5J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4I5J FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4i5j]] 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=4I5J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4I5J FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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">X-ray diffraction, [[Resolution|Resolution]] 2.091&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4i5k|4i5k]], [[4i5n|4i5n]]</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=CA:CALCIUM+ION'>CA</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PPP2R3A, PPP2R3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=4i5j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i5j OCA], [https://pdbe.org/4i5j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4i5j RCSB], [https://www.ebi.ac.uk/pdbsum/4i5j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4i5j ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4i5j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i5j OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4i5j RCSB], [http://www.ebi.ac.uk/pdbsum/4i5j PDBsum]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/P2R3A_HUMAN P2R3A_HUMAN] The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment.
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The B''/PR72 family of protein phosphatase 2A (PP2A) is an important PP2A family involved in diverse cellular processes, and uniquely regulated by calcium binding to the regulatory subunit. The PR70 subunit in this family interacts with cell division control 6 (Cdc6), a cell cycle regulator important for control of DNA replication. Here, we report crystal structures of the isolated PR72 and the trimeric PR70 holoenzyme at a resolution of 2.1 and 2.4 A, respectively, and in vitro characterization of Cdc6 dephosphorylation. The holoenzyme structure reveals that one of the PR70 calcium-binding motifs directly contacts the scaffold subunit, resulting in the most compact scaffold subunit conformation among all PP2A holoenzymes. PR70 also binds distinctively to the catalytic subunit near the active site, which is required for PR70 to enhance phosphatase activity toward Cdc6. Our studies provide a structural basis for unique regulation of B''/PR72 holoenzymes by calcium ions, and suggest the mechanisms for precise control of substrate specificity among PP2A holoenzymes.
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Structure of the Ca(2+)-dependent PP2A heterotrimer and insights into Cdc6 dephosphorylation.,Wlodarchak N, Guo F, Satyshur KA, Jiang L, Jeffrey PD, Sun T, Stanevich V, Mumby MC, Xing Y Cell Res. 2013 Jul;23(7):931-46. doi: 10.1038/cr.2013.77. Epub 2013 Jun 11. PMID:23752926<ref>PMID:23752926</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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==See Also==
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</div>
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*[[Protein phosphatase 3D structures|Protein phosphatase 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Jeffery, P D]]
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[[Category: Large Structures]]
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[[Category: Shi, Y]]
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[[Category: Jeffery PD]]
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[[Category: Xing, Y]]
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[[Category: Shi Y]]
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[[Category: Ef hand]]
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[[Category: Xing Y]]
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[[Category: Hydrolase]]
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[[Category: Phosphatase regulatory subunit]]
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[[Category: Pp2a]]
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Current revision

PP2A PR70 Holoenzyme

PDB ID 4i5j

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