4kk3
From Proteopedia
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| - | {{STRUCTURE_4kk3| PDB=4kk3 | SCENE= }} | ||
| - | ===YwlE arginine phosphatase - wildtype=== | ||
| - | {{ABSTRACT_PUBMED_23770242}} | ||
| - | == | + | ==YwlE arginine phosphatase - wildtype== |
| - | [[http://www.uniprot.org/uniprot/ | + | <StructureSection load='4kk3' size='340' side='right'caption='[[4kk3]], [[Resolution|resolution]] 1.70Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4kk3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KK3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KK3 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]] 1.7Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=4kk3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kk3 OCA], [https://pdbe.org/4kk3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kk3 RCSB], [https://www.ebi.ac.uk/pdbsum/4kk3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kk3 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PAP_BACSU PAP_BACSU] Catalyzes the specific dephosphorylation of phosphoarginine residues in a large number of proteins. Counteracts the protein arginine kinase McsB in vivo. Can dephosphorylate CtsR-P; thus, can restore the DNA-binding ability of the CtsR repressor by reversing the McsB-mediated phosphorylation. Is the only active pArg phosphatase present in B.subtilis. Exhibits almost no activity against pSer, pThr, or pTyr peptides. Appears to play a role in B.subtilis stress resistance. Protein arginine phosphorylation has a physiologically important role and is involved in the regulation of many critical cellular processes, such as protein homeostasis, motility, competence, and stringent and stress responses, by regulating gene expression and protein activity.<ref>PMID:22517742</ref> <ref>PMID:23770242</ref> <ref>PMID:24263382</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Many cellular pathways are regulated by the competing activity of protein kinases and phosphatases. The recent identification of arginine phosphorylation as a protein modification in bacteria prompted us to analyze the molecular basis of targeting phospho-arginine. In this work, we characterize an annotated tyrosine phosphatase, YwlE, that counteracts the protein arginine kinase McsB. Strikingly, structural studies of YwlE reaction intermediates provide a direct view on a captured arginine residue. Together with biochemical data, the crystal structures depict the evolution of a highly specific phospho-arginine phosphatase, with the use of a size-and-polarity filter for distinguishing phosphorylated arginine from other phosphorylated side chains. To confirm the proposed mechanism, we performed bioinformatic searches for phosphatases, employing a similar selectivity filter, and identified a protein in Drosophila melanogaster exhibiting robust arginine phosphatase activity. In sum, our findings uncover the molecular framework for specific targeting of phospho-arginine and suggest that protein arginine (de)phosphorylation may be relevant in eukaryotes. | ||
| - | + | Structural basis for recognizing phosphoarginine and evolving residue-specific protein phosphatases in gram-positive bacteria.,Fuhrmann J, Mierzwa B, Trentini DB, Spiess S, Lehner A, Charpentier E, Clausen T Cell Rep. 2013 Jun 27;3(6):1832-9. doi: 10.1016/j.celrep.2013.05.023. Epub 2013, Jun 13. PMID:23770242<ref>PMID:23770242</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | < | + | </div> |
| + | <div class="pdbe-citations 4kk3" style="background-color:#fffaf0;"></div> | ||
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| + | ==See Also== | ||
| + | *[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Bacillus subtilis subsp. subtilis str. 168]] | [[Category: Bacillus subtilis subsp. subtilis str. 168]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Clausen | + | [[Category: Clausen T]] |
| - | [[Category: Fuhrmann | + | [[Category: Fuhrmann J]] |
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Current revision
YwlE arginine phosphatase - wildtype
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