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. 2021 Jun 23;12:3883. doi: 10.1038/s41467-021-24199-1

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© The Author(s) 2021

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. 5 — a Comparison of ORC (left) and ORC–Cdc6 (right) in surface view showing that the binding of the Cdc6 to ORC leads to the assembly of three composite Mcm2-7 binding sites, which are absent in ORC itself. b, c Enlarged view of panel a showing the absence (b) and the presence (c) of the binding sites (dashed black circles) for the WHDs of Mcm3 and Mcm7. d A short α-helix of Orc1 AAA+ domain shifts by 5 Å upon Cdc6 binding to form the ATP-binding pocket of Cdc6. e The Cdc6 ATP binding site is formed by side chains from both Cdc6 and Orc1. Orc1 Arg-616 serves as the arginine finger for the ATP in Cdc6. ATPγS and surrounding residues are shown as sticks.