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. 2023 Jul 24;14:4445. doi: 10.1038/s41467-023-40096-1

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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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 1 — a Overview of the apCX3 heterodimer structure with important subdomains, regions, unique features for RAD51C (gold) and XRCC3 (teal), and bound ATP-mimic (magenta) highlighted. top, sketch of RAD51C and XRCC3 sequence with known motifs. b Structural superposition of the apCX3 core dimer with ATP-bound human RAD51 dimer (PDB 7EJC) to highlight the unique positioning of the XRCC3 NTD (teal) subdomain in the CX3 structure (see arrows). Dashed box, zoomed view of boxed area, rotated 90°, comparing the polymerization motif (PM) of RAD51 and XRCC3. c Comparison of a structural model of full-length hCX3 based on our apCX3 core and apRAD51C NTD structures to experimental SAXS data collected on hCX3.