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. 2019 Sep 26;9:13930. doi: 10.1038/s41598-019-50249-2

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© The Author(s) 2019

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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E. coli MtlR and HPr forms a stable heterotetramer. (A) The SEC-MALS analysis of ecHisMtlR (left) and the ecHisMtlR-HPr complex (right). Refractive index (RI) and light scattering (LS) signals were measured to determine protein concentration (top panels) and molar mass (bottom panels), respectively. (B) Structure of the ecMtlR monomer (green) in complex with HPr (yellow). The vpMtlR structure¹¹ (PDB 3BRJ, gray) is superposed on the ecMtlR structure. N- and C-termini and α-helices of both MtlRs are labeled. vpMtlR has an additional α-helix (α7 in gray) compared with ecMtlR, thus α8 of vpMtlR in gray and α7 of ecMtlR in green are structurally aligned.