View source for 2y09


==The cyanobacterial PP2C-like phosphatase tPphA requires three metals in the catalytic center for efficient catalysis==
<StructureSection load='2y09' size='340' side='right'caption='[[2y09]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2y09]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechococcus_elongatus Synechococcus elongatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y09 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Y09 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</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=MG:MAGNESIUM+ION'>MG</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=2y09 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y09 OCA], [https://pdbe.org/2y09 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2y09 RCSB], [https://www.ebi.ac.uk/pdbsum/2y09 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2y09 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8DGS1_THEVB Q8DGS1_THEVB] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Protein phosphatase M (PPM) regulates key signaling pathways in prokaryotes and eukaryotes. Novel structures of bacterial PPM members revealed three divalent metal ions in their catalytic centers. The function of metal 3 (M3) remained unclear. To reveal its function, we created variants of tPphA from Thermosynechococcus elongatus in all metal-coordinating residues, and multiple variants were created for the M3 coordinating Asp-119 residue. The structures of variants D119A and D193A were resolved, showing loss of M3 binding but unaffected binding of M1 and M2 in the catalytic center of D119A, with the nucleophilic water molecule in the correct place. The catalytic activity of this variant was highly impaired. This and further structure-function analyses showed that M3 is required for catalysis by providing a water molecule as a proton donor during catalysis. Mutation of the homologue Asp residue in human PP2Calpha also caused loss of function, suggesting a general requirement of M3 in PPM-catalyzed reactions.

A Third Metal Is Required for Catalytic Activity of the Signal-transducing Protein Phosphatase M tPphA.,Su J, Schlicker C, Forchhammer K J Biol Chem. 2011 Apr 15;286(15):13481-8. Epub 2011 Feb 10. PMID:21310952<ref>PMID:21310952</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2y09" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Synechococcus elongatus]]
[[Category: Forchhammer K]]
[[Category: Jiyong S]]
[[Category: Schlicker C]]