Fig. 8: The S267E mutation disrupts the stability of insert-1. | Nature Communications

Fig. 8: The S267E mutation disrupts the stability of insert-1.

From: Motor domain phosphorylation increases nucleotide exchange and turns MYO6 into a faster and stronger motor

Fig. 8

a MYO6 atomic model used in MD simulations. Insert-1 is highlighted in yellow. Atomic models of the insert-1 domain in WT (left inset) and S267E (right inset) mutant with key residues highlighted after energy minimization. b Snapshots of the insert-1 domain (orange) and 310 loop (magenta) after 1 μs for the WT (replica 2) (left) and S267E (replica 1) (right) trajectories. c Comparison of insert-1 and L310 loop conformations at 0 and 1 μs in WT (replica 2) (left) and S267E (replica 1) (right) mutant trajectories obtained by superposition of residues 260–280 around the insert-1 domain and L310 loop. d, e Probability distribution plots for d the distance between the sidechain oxygens of the indicated pairs of residues and e the RMSD (root mean square deviation) of the insert-1 domain (residues 278–303) and L310 loop (residues 308–312) for the WT and S267E mutant simulations. All distance plots include data from the final 200 ns of all three replicas.

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