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. 2020 Dec 18;11:6420. doi: 10.1038/s41467-020-20157-5

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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 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 Linear representation of the structure of HelD with a map of coloured domains and conserved sequence motifs (top), and a histogram of sequence identity (bottom). b The structure of HelD (bottom) coloured according to the schematic in panel a. SCA is shown in yellow, SF1 helicase-like domain 1 A in red, CA in dark grey, and SF1 helicase-like domain 2 A in orange. Conserved sequence motifs are shown in purple, with the Walker A/B ATP-binding site in cyan. c, shows a surface-rendered impression of HelD with the same colouring as in b. The bottom panel shows an expanded view of the boxed region in the top panel with a semi-transparent surface and conserved amino acids that form the ‘Trp cage’ shown as purple sticks, and the conserved Trp in dark green.