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. 2019 Jul 23;10:3286. doi: 10.1038/s41467-019-11120-0

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© The Author(s) 2019

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 — Sequence alignment of connectors essential in driving motor conformational changes–lack of canonical residues in PfMyoA. a Sequence comparison of several key elements involved in myosin mechanical transduction and allosteric communication. The consensus is represented on top of each sequence and the PfMyoA sequence is compared to other myosins. This comparison shows that the sequences of the Switch-2, Wedge, and Relay differ from the consensus. Consensus code: a is an aromatic residue, h a hydrophobic residue, x colored in red is an acidic residue. Residues important in allosteric communication in the motor are indicated in rectangles (blue rectangle if the residue is involved in a conserved interface, red rectangle if the residues are involved in interactions specific to PfMyoA). If the position is not conserved in PfMyoA, the residue is colored in dark red. To see how these residues affect the PfMyoA motor rearrangements along the cycle, see Fig. 4 and Supplementary Movie 2. b Switch-2/Wedge interactions in classical Myo2. c Conformational changes of two connectors before (PPS, transparent) and after (Rigor-like, plain) the powerstroke in Myo2. The Relay helix unkinks while the SH1-helix undergoes a piston-like movement using the canonical flexibility found at the fulcrum ^SH2-SH1Gly (pink ball)