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. 2021 Mar 25;12:1892. doi: 10.1038/s41467-021-22093-4

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© The Author(s) 2021

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. 3 — a Atomic model of filamentous PfAct1 while bound to PfMyoA with root mean square differences to the bare PfAct1 filament structure mapped in thickness and color, from 0–2.5 Å. b The D-loop shows only minor structural differences in the bound (cyan) compared to the bare (chocolate red) filament (PDB code 5OGW; https://www.rcsb.org/structure/5OGW)¹¹ with the largest difference occurring at residue E51. In the decorated filament, the conformation of the sidechain of E51 is reoriented in order to establish a polar contact of with S558 from the HTH of PfMyoA (dark blue). c The plug conformation is identical in both structures and the specific polar interactions are conserved. d Comparison of the normalized atomic temperature factors between the bound (left) and unbound (right) PfAct1structures. e Jasplakinolide (JAS) is well defined in the density map of the PfMyoA bound PfAct1 structure.