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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. 7 — a Relative orientation of two TbIMPDH monomers located in the ASU, estimated by the approximate angle spanned by the two beta sheets of the CBS motifs in each Bateman domain, as indicated by the dashed line. The finger domains are highlighted (orange/red), the catalytic residues (cyan), and the bound nucleotides (gray) are shown as spheres. b Detailed view on the interface formed by the adjacent Bateman domains (green/blue, cartoon representation) within the TbIMPDH dimer. Residues involved in the dimer interaction (yellow dashes) and ATP/GMP molecules are shown as sticks. The displayed 2F_oF_c-electron density of ATP and GMP is countered at 1.0 sigma. c Cartoon representation of the octamer assembly of TbIMPDH monomers, as observed within the in cellulo crystals and corresponding space group, in different views rotated by 90°. Four dimers are forming an octamer around the 4-fold symmetry axis. The dimeric building blocks observed within the ASU are individually colored. Bound nucleotides are shown in a gray spheres representation.