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. 2015 Jan 20;5(8):863–885. doi: 10.4161/21505594.2014.983404

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© 2014 The Author(s). Published with license by Taylor & Francis Group, LLC

© David P Wright and Andrew T Ulijasz

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. The moral rights of the named author(s) have been asserted.

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Figure 9. — Comparison of CovR and VraR Receiver (REC) domain phosphorylation sites. (A) (left panel) Cartoon representation of an atomic model of the CovR REC domain. The model was created with Swiss-Model (ref.¹⁶¹) using the CovR sequence from S. agalactiae and the PhoP structure from M. tuberculosis (PDB code 3R0J; ref.¹⁶⁵) as a molecular template. Phosphorylated residues are shown in red. The conserved histidine kinase phosphorylated aspartate (Asp53) is shown in green. Residues that would potentially pose a steric clash with the phosphorylated Thr65 are shown in yellow. (right panel) Surface representation of the left panel rotated 180 degrees. Notice that Thr65 is solvent accessible, but resides in a deep cleft within the interior of the protein. (B) The VraR atomic (REC) structure taken from ref.⁶³ showing the eSTK-regulated Thr119 (colored red) and potential residues that might clash with it in its phosphorylated form (colored yellow). The conserved Asp55 is shown in green.