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. 2017 Aug 4;8:190. doi: 10.1038/s41467-017-00176-5

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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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Fig. 2 — Binding of OM stabilizes a specific primed position of the myosin lever arm and does not affect the motor domain conformation. a The features of the motor domain including the position of the subdomains (Nter (grey), U50 (blue), L50 (white)) and key connectors are similar for the OM-S1-PPS (multi-colored) and the APO-MD-PPS (pink) structures. b Superimposition of the OM-S1-PPS (multi-colored) structure with the Argopecten skeletal myosin II in the PPS state (1QVI¹³ , purple). c Comparison of the relay and the converter in the APO-MD-PPS structure (pink) and the OM-S1-PPS (multi-colored). The relay (yellow) is displaced by ~ 6 Å, and the converter subdomain (green) is rotated (15°) and translated (~ 4 Å). Overall, OM binding stabilizes a conformation of the converter that forms a specific “PPS” allosteric binding site for OM and maintains the converter in a primed position. d Detail of the OM “PPS” binding pocket. Closure of the allosteric site (black arrows) stabilizes interactions between OM and converter residues, such as Arg712 and Ile713 as well as His492 which adopts a new conformation to interact with OM