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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. 4 — Structural fluctuations of domains in SecA proteins. Normal mode analyses (NMA) of both the open (a) and the wide open (b) conformations of SecA. The figure shows the intrinsic movements of each domain. The arrow lengths and colour are correlated to their fluctuations. In both structures the pre-protein binding domain (PBD; yellow) moves towards the helical wing domain (HWD). The major difference between the two conformations regarding their intrinsic movements refers to the IRA2 and HWD which move towards the PBD in the open conformation (a), or away from the PBD in the wide open state of SecA (b)