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. 2014 Sep 17;5:495. doi: 10.3389/fmicb.2014.00495

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Copyright © 2014 Shi, Pigeonneau, Ravikumar, Dobrinic, Macek, Franjevic, Noirot-Gros and Mijakovic.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Phosphorylation of PrkD by PrkC and HprK/P. (A) Identification of phosphorylated residues by mass spectrometry. Fragmentation spectra are shown for the three modified peptides, bearing the residues threonine 213, threonine 241, and serine 243 phosphorylated by PrkC, and serine 148 phosphorylated by HprK/P. (B) Mapping of the phosphorylated residues on the structural model of PrkD obtained by SWISS-MODEL (surface representation). The phosphorylated residues are shown in red. Residues in the activation loop are in blue, and the catalytic site is in yellow.