4mew: Difference between revisions

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-'''Unreleased structure'''
+==Structure of the core fragment of human PR70==
+<StructureSection load='4mew' size='340' side='right' caption='[[4mew]], [[Resolution|resolution]] 1.99&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4mew]] is a 1 chain structure. 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>
+</td></tr><tr><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><br>
+<tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
+<tr><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>
+<table>
+<div style="background-color:#fffaf0;">
+== 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.
-The entry 4mew is ON HOLD  until Paper Publication
+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<ref>PMID:25007185</ref>
-Authors: Dovega, R.B., Quistgaard, E.M., Tsutakawa, S., Anandapadamanaban, M., Low, C., Nordlund, P.
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-Description: Structure of the core fragment of human PR70
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Anandapadamanaban, M.]]
+[[Category: Dovega, R B.]]
+[[Category: Low, C.]]
+[[Category: Nordlund, P.]]
+[[Category: Quistgaard, E M.]]
+[[Category: Tsutakawa, S.]]
+[[Category: Calcium binding]]
+[[Category: Cell cycle]]
+[[Category: Ef-hand]]
+[[Category: Hydrolase]]
+[[Category: Metal binding protein]]
+[[Category: Protein phosphatase]]