4KK4
YwlE arginine phosphatase - C7S mutant with phosphorylated active site serine
Summary for 4KK4
| Entry DOI | 10.2210/pdb4kk4/pdb |
| Related | 4KK3 |
| Descriptor | Low molecular weight protein-tyrosine-phosphatase YwlE (2 entities in total) |
| Functional Keywords | protein modification, arginine phosphorylation, arginine dephosphorylation, phosphatase reaction intermediate, lmw ptp, phosphorylation at ser6, hydrolase |
| Biological source | Bacillus subtilis subsp. subtilis |
| Total number of polymer chains | 1 |
| Total formula weight | 17116.39 |
| Authors | Fuhrmann, J.,Clausen, T. (deposition date: 2013-05-05, release date: 2013-07-03, Last modification date: 2013-07-17) |
| Primary citation | Fuhrmann, J.,Mierzwa, B.,Trentini, D.B.,Spiess, S.,Lehner, A.,Charpentier, E.,Clausen, T. Structural basis for recognizing phosphoarginine and evolving residue-specific protein phosphatases in gram-positive bacteria. Cell Rep, 3:1832-1839, 2013 Cited by PubMed 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. PubMed: 23770242DOI: 10.1016/j.celrep.2013.05.023 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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