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. Author manuscript; available in PMC: 2026 Apr 11.
Published in final edited form as: Biochem Biophys Res Commun. 2026 Feb 10;807:153439. doi: 10.1016/j.bbrc.2026.153439

Fig. 3.

Fig. 3.

Location of potentially-interacting residues in the relay and converter domains modeled using the crystal structures of scallop myosin S-1 in the pre- (PDB 1QVI; [15]) and post (actin-detached)- (PDB 1KK8; [16]) power stroke states. A. Indirect flight muscle myosin isoform (IFI) in pre- (left) and post-power stroke (right) states. Relay domain polar residue N509 (red) potentially interacts with the converter domain basic residue R759 (green) best in the post-power stroke state. The relay domain acidic residue D511 (grey) appears to interact with the converter domain basic residue R759 in the post-power stroke state, but not in the pre-power stroke state. B. EMB in the pre- (left) and post-power stroke (right) states. Relay domain acidic residue D509 (red) interacts best with the converter domain basic residue R759 (green) in the post-power stroke state. The relay domain hydrophobic residue A511 (grey) appears unlikely to interact with the converter domain basic residue R759 in either state. C. IFI relay domain mutations inserted into the EMB isoform in the pre- (left) and post-power stroke (right) states. Relay domain polar residue D509 N (red) interacts best with converter domain basic residue R759 (green) in the post-power stroke (right) state. Relay domain acidic residue A511D (grey) may weakly interact with the converter domain basic residue R759 in the post-power stroke state. The chicken skeletal muscle myosin numbering system was used for all residue numbers [7].