Structural Basis for Recognizing Phosphoarginine and Evolving Residue-Specific Protein Phosphatases in Gram-Positive Bacteria

Structural Basis for Recognizing Phosphoarginine and Evolving Residue-Specific Protein Phosphatases in Gram-Positive Bacteria

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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 Accessories 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 Board Games 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.