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. 2022 Feb 8;12:2061. doi: 10.1038/s41598-022-06073-2

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© The Author(s) 2022

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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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Domain organization of phage CBA120 TSP1-4 and recombinant TSP fragments. The N-terminal baseplate anchor domain (AD) is colored magenta. Three T4 gp10-like domains of TSP4 (XD1, XD2 and XD3) and two of TSP2 (XD2 and XD3) are colored different shades of brown. Domain linkers are indicated as red double arrows. The helical neck separating the head region from the TSP body/catalytic domains is indicated as magenta double arrows. The head domains, D1 and D2, are colored blue and yellow, respectively. The D3’ domain inserted after the neck in TSP2 and TSP4 is colored pink. The β-helix domain, D3, and the C-terminal domain, D4, are colored green and cyan, respectively. Structures of the D1-D4 regions have been determined for all four TSPs^2,4–6. The AD-XD1-XD2-XD3 region is the focus of the current study.