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| | <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=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4mew]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MEW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MEW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4mew]] 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=4MEW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MEW FirstGlance]. <br> |
| - | </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" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <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'>[https://proteopedia.org/fgij/fg.htm?mol=4mew FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mew OCA], [https://pdbe.org/4mew PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mew RCSB], [https://www.ebi.ac.uk/pdbsum/4mew PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mew ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PPP2R3B, PPP2R3L ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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 == |
| - | [[http://www.uniprot.org/uniprot/P2R3B_HUMAN 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. | + | [https://www.uniprot.org/uniprot/P2R3B_HUMAN 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. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 4mew" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4mew" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Protein phosphatase 3D structures|Protein phosphatase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Anandapadamanaban, M]] | + | [[Category: Anandapadamanaban M]] |
| - | [[Category: Dovega, R B]] | + | [[Category: Dovega RB]] |
| - | [[Category: Low, C]] | + | [[Category: Low C]] |
| - | [[Category: Nordlund, P]] | + | [[Category: Nordlund P]] |
| - | [[Category: Quistgaard, E M]] | + | [[Category: Quistgaard EM]] |
| - | [[Category: Tsutakawa, S]] | + | [[Category: Tsutakawa S]] |
| - | [[Category: Calcium binding]]
| + | |
| - | [[Category: Cell cycle]]
| + | |
| - | [[Category: Ef-hand]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Metal binding protein]]
| + | |
| - | [[Category: Protein phosphatase]]
| + | |
| 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 PubMed
Protein 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.
See Also
References
- ↑ Dovega R, Tsutakawa S, Quistgaard EM, Anandapadamanaban M, Low C, Nordlund P. Structural and Biochemical Characterization of Human PR70 in Isolation and in Complex with the Scaffolding Subunit of Protein Phosphatase 2A. PLoS One. 2014 Jul 9;9(7):e101846. doi: 10.1371/journal.pone.0101846. eCollection, 2014. PMID:25007185 doi:http://dx.doi.org/10.1371/journal.pone.0101846
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