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. 2017 May 3;7:1385. doi: 10.1038/s41598-017-01497-7

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© The Author(s) 2017

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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Schematic of the transition from dark-adapted to light-adapted state of YF1 and proposed signal transduction mechanism. (A) The outward tilt of the LOV domains in a hinge-like motion (red) causes separation of the N-termini of the coiled-coil linker (green arrows). (B) Separation of the N-termini would induce torque and left-handed supercoiling of the coiled-coil linker. (C) As a result, the C-termini of the linker helices (inset) would be rotated relative to the C2 axis of the coiled coil, causing both a rotation of the LOV dimer relative to the histidine kinase effector (dotted line) and an angular movement of the helices themselves. To illustrate the resultant angular displacement, within each helix two positions separated by one residue are highlighted in green and red, respectively.