4KK3

YwlE arginine phosphatase - wildtype

Summary for 4KK3

• Entry DOI: 10.2210/pdb4kk3/pdb
• Related: 4KK4
• Descriptor: Low molecular weight protein-tyrosine-phosphatase YwlE, PHOSPHATE ION (3 entities in total)
• Functional Keywords: protein modification, arginine phosphorylation, arginine dephosphorylation, phospho-proteome, lmw-ptp, hydrolase
• Biological source: Bacillus subtilis subsp. subtilis
• Total number of polymer chains: 1
• Total formula weight: 17205.91

Authors

Fuhrmann, J.,Clausen, T. (deposition date: 2013-05-05, release date: 2013-07-03, Last modification date: 2024-11-27)

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

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: 23770242
DOI: 10.1016/j.celrep.2013.05.023

Experimental method

X-RAY DIFFRACTION (1.7 Å)