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- W4254754302 abstract "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. Copyright © 2013 The Authors. Published by Elsevier Inc. All rights reserved. PMID: 23770242" @default.
- W4254754302 created "2022-05-12" @default.
- W4254754302 creator A5023564164 @default.
- W4254754302 date "2013-07-24" @default.
- W4254754302 modified "2023-09-27" @default.
- W4254754302 title "Faculty Opinions recommendation of Structural basis for recognizing phosphoarginine and evolving residue-specific protein phosphatases in gram-positive bacteria." @default.
- W4254754302 doi "https://doi.org/10.3410/f.718042611.793480769" @default.
- W4254754302 hasPublicationYear "2013" @default.
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