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. 2020 Dec 17;10:22253. doi: 10.1038/s41598-020-79226-w

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© The Author(s) 2020

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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The 3D structure of the wild-type flagellin FliC, the genetically engineered FliC-NikR_C and the FliC-NikR_C tetramer that is spontaneously formed in solution. Each monomer unit of the FliC-NikR_C tetramer has one HA Ni-binding site. Note that the D0 and partly the D1 domain forms a disordered region displaying high flexibility. While the structure of FliC (PDB ID: 1UCU) and NikR C-domain (PDB ID: 3BKU) is well established by electron microscopy, the shown structure of monomeric and tetrameric FliC-NikR_C is based on modeling using the Chimera Software⁶⁵. Due to the conformational variability in its disordered arms, only a hypothetical structure could be shown for the FliC-NikR_C tetramer.