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. 2020 Nov 23;11:5945. doi: 10.1038/s41467-020-19695-9

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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. 2 — a Structural overlay of the small domains of AncCDT-3/L188 (purple, PDB 5JOS), AncCDT-5 (green) and PaCDT (white, PDB 3KBR). The Tyr177Gln substitution that occurs between AncCDT-3 and AncCDT-5 contributes to the repositioning of Glu173. b Structural alignment of the active sites of AncCDT-3/L188 (purple, PDB 5JOS), AncCDT-5 (green) and PaCDT (PDB 3KBR, white). The small domain (residues 99–194) and large domain (residues 1–98 and 195–236) of AncCDT-3/L188 and AncCDT-5 were individually aligned with the corresponding domains of PaCDT. The sidechains of the 15 inner-shell residues identified by Clifton et al.⁴⁰ are shown as sticks (Gly131 not shown), highlighting identical active site residues and side-chain conformations between AncCDT-5 and PaCDT. The HEPES molecules present in the crystal structures are omitted for clarity. c The locations of the substitutions (green spheres) between AncCDT-5 and PaCDT are shown projected onto the structure of PaCDT (PDB 3KBR).