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. 2019 Feb 4;9:1261. doi: 10.1038/s41598-018-37417-6

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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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The dimeric structure of Ts2631 endolysin shows a 3D domain swap via the N-terminus. (A) Asymmetric unit of Ts2631 endolysin showing two protein molecules, which are highlighted in a ribbon representation. The dimer is interconnected by an elongated and largely unstructured N-terminus (residues 1–20), which carries seven positively charged residues (six arginines, one lysine; shown in stick representation), most of which are pointing towards the same direction (residues in stick representation are denoted by type and numbers). The structure represents a 3D domain swap of two interconnected monomers. (B) Molecular interactions between the N-terminus of monomer A (in blue) and the globular domain of monomer B (in orange) are marked by dashed lines. Interacting residues are marked in the same color as their respective domains and numbered according to their position in the sequence.