4mew: Difference between revisions
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==Structure of the core fragment of human PR70== | ==Structure of the core fragment of human PR70== | ||
<StructureSection load='4mew' size='340' side='right' caption='[[4mew]], [[Resolution|resolution]] 1.99Å' scene=''> | <StructureSection load='4mew' size='340' side='right' caption='[[4mew]], [[Resolution|resolution]] 1.99Å' scene=''> | ||
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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>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4mew FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mew OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4mew RCSB], [http://www.ebi.ac.uk/pdbsum/4mew PDBsum]</span></td></tr> | <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=4mew FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mew OCA], [http://pdbe.org/4mew PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4mew RCSB], [http://www.ebi.ac.uk/pdbsum/4mew PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4mew ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4mew" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 01:38, 5 August 2016
Structure of the core fragment of human PR70Structure of the core fragment of human PR70
Structural highlights
Function[P2R3B_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. Publication Abstract from PubMedProtein Phosphatase 2A (PP2A) is a major Ser/Thr phosphatase involved in the regulation of various cellular processes. PP2A assembles into diverse trimeric holoenzymes, which consist of a scaffolding (A) subunit, a catalytic (C) subunit and various regulatory (B) subunits. Here we report a 2.0 A crystal structure of the free B/PR70 subunit and a SAXS model of an A/PR70 complex. The crystal structure of B/PR70 reveals a two domain elongated structure with two Ca2+ binding EF-hands. Furthermore, we have characterized the interaction of both binding partner and their calcium dependency using biophysical techniques. Ca2+ biophysical studies with Circular Dichroism showed that the two EF-hands display different affinities to Ca2+. In the absence of the catalytic C-subunit, the scaffolding A-subunit remains highly mobile and flexible even in the presence of the B/PR70 subunit as judged by SAXS. Isothermal Titration Calorimetry studies and SAXS data support that PR70 and the A-subunit have high affinity to each other. This study provides additional knowledge about the structural basis for the function of B containing holoenzymes. Structural and Biochemical Characterization of Human PR70 in Isolation and in Complex with the Scaffolding Subunit of Protein Phosphatase 2A.,Dovega R, Tsutakawa S, Quistgaard EM, Anandapadamanaban M, Low C, Nordlund P PLoS One. 2014 Jul 9;9(7):e101846. doi: 10.1371/journal.pone.0101846. eCollection, 2014. PMID:25007185[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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