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. 2020 Jan 30;11:620. doi: 10.1038/s41467-020-14484-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 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. 6 — a Cartoon and surface representation of superposed monomers A from TbIMPDH-ATP1/GMP2 (green) and from AgIMPDH-ATP1/GDP2/GDP3 (blue, PDB 5TC3). Nucleotide atoms are shown as spheres. Both structures adopt an almost superimposable relative domain orientation. b Detailed view of the linker region (orange) between the Bateman (dark green) and the catalytic domains (light green) of TbIMPDH-ATP1/GMP2. The flipped conformation of GMP enables a direct interaction with residue Arg101 in the catalytic domain. Further stabilization is provided by an interaction of Arg107 and Arg223. ATP atoms are shown as spheres, while GMP and the GMP-binding residues as well as interface stabilizing residues are represented as sticks. Key interactions are shown as yellow dashes.