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. 2018 Sep 3;1:130. doi: 10.1038/s42003-018-0133-4

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© The Author(s) 2018

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. 2 — The pre-protein binding domain (PBD) moves closer to the helical wing domain (HWD) upon adenosine triphosphate (ATP) binding. Histograms of the single-molecule Förster resonance energy transfer (smFRET) data obtained with SecA 329C-704C, in the absence (top panel) and the presence of ATP (bottom panel). The data can be fitted best with two Gaussian distributions. The distance between the two fluorophores in the PBD and in the HWD decreases when ATP is present from 6.5 nm to 5.5 nm, indicating that the PBD moves towards the HWD. Insets show the position of the fluorescent labels in SecA. To illustrate the movement of the PBD, the atomic SecA structures 1TF2 (top) and 1M74 (bottom) are shown. The distance between the PBD at residue 329 (red dot) and the HWD at 704 (green dot) is highlighted with arrows and is 5.6 nm in the B. subtilis open structure (1TF2) and 4.5 nm in the wide open structure (1M74) between the corresponding residues (D309 and V658)