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. 2019 Jul 9;9:9896. doi: 10.1038/s41598-019-45885-7

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© The Author(s) 2019

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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Model of the structural movement in CraCRY from the fully oxidized to the hydroquinone state of the FAD based on the HDX data. In between, the neutral semiquinone state is formed (FADH°), but we have no structural information addressing this state. In the shown model, the C-terminal extension (CTE, red) is located over the protein surface and is partly structured. We propose that an unknown signaling partner X (light blue) can bind to CraCRY during the night, when it is located over the whole cell body. During the day, the hydroquinone state is forming (FADH⁻). Because of the radical pair formation [Y373° and FADH°] during photoreduction, the H-bond network between α22, D323 and D321 is disrupted which leads to a movement of the helix and therefore a change in the CTE. The structured region in the CTE gets unfolded and factor X is getting released.