Fig. 2: Role of the proximal Myo6 sequence in the stabilization of the off-state.
From: How myosin VI traps its off-state, is activated and dimerizes
a Model of Myo6 opening/back-folding. Back-folding requires the SAH to fold back on the 3HB. The L926 residue (red cross) leads to deafness when mutated into Gln39. (Insert) Mutations of the apolar residues at the N-terminus of the SAH to turn Myo6 into a constitutive monomer16 (SAHmimic). b Dimensionless Kratky plot representation from SEC-SAXS. FLMyo6 in NF/high salt is pictured in black. In the presence of ADP.AlF4 (ADP.Pi analog), FLMyo6 (L926Q) (yellow) and FLMyo6 (SAHmimic) (light blue) spectrums correspond to an elongated shape, as opposed to FLMyo6 WT (green). c Rg of FLMyo6 WT, L926Q and SAHmimic determined by SEC-SAXS experiments (n = 1) in the presence of ADP.AlF4 (ADP.Pi analog) and FLMyo6 in NF/high salt. Rg values were extracted from linear fits of the Guinier plots shown in Supplementary Fig. 1C using primusqt (ATSAS suite50). Mean ± SD. d Actin-activated ATPase rate of FLMyo6 WT, L926Q, SAHmimic and MDIns2 (n = 6). Mean ± SD. (b-d) Source data are provided as a Source Data file.
