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. 2017 Jun 23;8:15720. doi: 10.1038/ncomms15720

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Copyright © 2017, The Author(s)

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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Cdt1 binds to the side of Mcm2 and Mcm6, interacting both with N-terminal and AAA+ ATPase elements. Cdt1 stabilizes a topologically open left-handed spiral configuration of MCM, with a discontinuity between the Mcm5 and Mcm2 subunits, disrupting a functionally essential AAA+ ATPase site. DNA recruitment mediated by ORC and Cdc6 (OCCM formation) planarizes the MCM ring, reconstituting the Mcm5–2 ATPase site, which becomes competent for ATP hydrolysis. Conversion to a post-catalytic, loaded MCM involves the clockwise rotation of the AAA+ ATPase tier. This conformational change probably disrupts a Cdt1 docking site on Mcm2, promoting ATPase-dependent Cdt1 ejection.