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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. 2 — a Atomic model of actin-bound PfMyoA motor domain with root mean square differences to the rigor-like unbound structure mapped in thickness and color, from 0–5.5 Å. Only residues present in both structures are shown. The hypertrophic cardiomyopathy loop (HCM), loop 4 (L4) and the upper and lower 50 kDa domains (U50, L50) are labeled. b Comparison of the normalized atomic temperature factors between the bound (upper panel) and unbound (lower panel) structures. The region shown corresponds to the box in A. c Density map and atomic model in the active site of PfMyoA shows without ambiguity the absence of nucleotide. There is no density in the cavity (black dashed lines) composed by the Switch-1 (green), Switch-2 (orange) and the P-loop (purple). d The density map and atomic model of the actin binding cleft located between the upper 50 kDa (U50, in blue) and the lower 50 kDa (L50, pink) domains.