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. 2023 Jun 2;14:3200. doi: 10.1038/s41467-023-38793-y

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© The Author(s) 2023

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. 10 — A Ribbon-surface representation of apo dParg. ADP-ribose dimer (yellow) of the aligned hPARG:ADP-ribose dimer complex structure is given to highlight the active site. Structural features important for catalysis are highlighted: accessory-domain loops 1 and 2, AD-loop 1 and 2; catalytic loop, loop 1; diphosphate binding loop, loop 2; tyrosine clasp, Tyr loop. B Ribbon representation of structural alignment of PARG domains from indicated species (Drosophila, red; human, yellow; mouse, orange; T. thermophile, white). The catalytic residues (Glu340/Glu341 in dParg) are highlighted in black. C Ribbon-liquorice representation of loop 1-AD-loop 1 interaction of Drosophila, human, and T. thermophile PARGs. Polar interactions are highlighted as black dotted lines and water molecules involved in the interaction as red spheres.