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. 2017 Nov 23;46(1):456–472. doi: 10.1093/nar/gkx1164

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© The Author(s) 2017. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com

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Figure 4. — Active site and functional studies on catalytic residues in RcsB. (A) Detail of the active site for RcsB_crossed (in pink) superposed with RcsB_BeF (in cyan). Catalytic residues as well as the sulfate ion (SO₄²⁻ labeled as SO₄) and BeF₃⁻(labeled as BeF) are shown as sticks. (B) Another view of the active site in RcsB_crossed (pink for one subunit and purple for the other). Residue E170 (in purple) from the DBD of the other subunit contributes to the active site. Catalytic and relevant residues are shown as sticks together with the sulfate ion (SO₄) and a water molecule (W). (C) Phosphorylation assays of WT and mutants of RcsB with AcP³². Phosphorylation was followed at 5, 10, 20, 40 and 60 min and was evaluated with the MultiGauge software (Fuji). (D) EMSAs of RcsB WT and mutant forms with P1_flhDC were performed in the absence and presence of 50 mM of AcP.