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. 2022 Jan 10;13:26. doi: 10.1038/s41467-021-26583-3

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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 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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Fig. 8 — a The predicted oligomerization interface at the beginning of α2 helix and the end of α4 helix of FsSTING (orange, PDB: 6WT4) are indicated and colored in red. By contrast, PcSTING (green) protomer uses the α5 helix to interact with the whole α2 helix of the adjacent PcSTING protomer. b The PcSTING and FsSTING dimers are superimposed. The orientation of α3 and α4 helix and thereby the predicted α3-α4 loop of FsSTING (red dashed lines) are different from those of PcSTING. c Multiple sequence alignment of four representatives of Class I bacterial STING proteins. d Multiple sequence alignment of four representatives of Class II bacterial STING proteins. The predicted oligomerization interfaces in FsSTING are highlighted by red frames.