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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 crystal structure of Ts2631 endolysin shows a conserved peptidoglycan binding site. (A) Structure of the globular protein presented in a cartoon representation with the extended N-terminal tail comprising a short α-helix, α1 (marked NT and α1). The secondary structure assignment to the mixed α/β structure is α1/β1/β2/α2/β3/β4/α3/β5. The β-sheet is sandwiched between helices α2 and α4, collectively enclosing the active site with the tetragonally coordinated zinc ion (zinc ion represented by a gray sphere; residues are shown in stick representations) in the center of the structure. (B) Surface representation of Ts2631 endolysin demonstrating positively charged patches at the N-terminus and around the active site, which is formed by residues His30, His131, Cys139 and a water molecule (W; blue sphere). (C) Expanded view of the active site in the same perspective as in (A,B), with the active site residues numbered and the zinc ion marked. All structure figures were prepared using PYMOL (www.pymol.org).