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. 2022 Jul 14;13:4105. doi: 10.1038/s41467-022-31678-6

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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. 3 — a Double-stranded DNA sequence present in the crystal structure is shown, with the consensus sequence underlined. The numbers are present to identify each nucleotide of the consensus. Residues that contact the DNA are listed, with dashed lines indicating interactions with the DNA bases, while solid lines designate residues that contact the DNA backbone. All polar contacts shown are 3.2 Å or less, and an asterisk indicates contacts that are only observed in the higher resolution selenomethionine structure. Residues are color-coded as in Fig. 1a, and the arrow indictates the direction of transcription. b Interactions between R45, Q46, and W50 of the α3 helix in the HTH domain and DNA bases are shown. c Interactions between the Stoperator domain and DNA bases. At the beginning of this domain, the η1 3₁₀ helix properly positions K75, D78, and K79 to contact bases of the DNA. K81 sits at the base of the α5 helix. R108 in the α6 helix is properly positioned to bind DNA via an interaction (colored red) with D104. In both panels b, c, the protein and DNA are colored coded as in Fig. 1a.