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. 2017 Jul 19;7:5860. doi: 10.1038/s41598-017-06289-7

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© The Author(s) 2017

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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c-di-GMP binds to Ethr at Q125, R181, E190. (a). Docking model analysis for the binding of c-di-GMP to Ethr. Ethr was docked to c-di-GMP, c-di-AMP, cGMP, and CNS (as a positive control). The docking data is shown in the table (left). In the Ethr-c-di-GMP docking model, c-di-GMP (middle) is mediated at Watson-Crick (WC) edge of guanine bases by glutamic acid E190, and at phosphate group by arginine R181 and glutamine Q125. The PDB code of Ethr crystal structure used for the Ethr-c-di-GMP docking model is 1U9O. (b). UV cross-linking assay for validating the binding of Ethr mutants to c-di-GMP. Ethr and mutants of Ethr^Q125A, Ethr^R181A, Ethr^E190A, were co-incubated with various concentration of biotinylation c-di-GMP. (c). BLI assay for validating the binding of Ethr mutants to c-di-GMP. Bio-c-di-GMP immobilized on streptavidin coated biosensor and co-incubated with various concentrations of Ethr or mutants.