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. 2021 Sep 21;11:18693. doi: 10.1038/s41598-021-98155-w

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© The Author(s) 2021

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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Structure of Bsp-lig bound to post-ligation product DNA. (A) Overall structure with latch region highlighted in magenta. Inset shows Bsp-lig active site with ligated nucleotides in DNA substrate indicated in red. AMP in cyan and key active site residues of Bsp-lig as green sticks. (B) Structure of ChlV-lig bound to DNA with latch highlighted in lime. (C) Structure of Ame-lig bound to DNA. (D) Superposition of latch regions from Bsp-lig (magenta) and ChlV-lig (lime) with key DNA-interacting residues shown as sticks. (E) Detailed view of interactions of Bsp-lig latch (magenta, top) and ChlV-lig latch (lime, lower) with DNA. DNA nucleotides and protein side-chains involved in interactions are shown as sticks, hydrogen bonds and salt bridges are indicated with yellow dashed lines. (F) Sequence logo of latch region for 28 Bsp-lig homologs (top) and alignment between latches of Bsp-lig and ChlV-lig (lower) with fully-conserved residues highlighted in red and synonymous differences indicated in red text.