Abstract
A cluster of basic residues on the surface of actin (K326, K328 and R147) are needed for F-actin to bind to acidic residues on tropomyosin in the blocked- and closed-states of the muscle thin filament (Li et al., 2011; Lehman et al., 2013; Orzechowski et al., 2013; Fischer et al., 2016). However, the binding of tropomyosin to actin is necessarily weak so that regulatory transitions across actin can proceed at low-energy cost. We propose that negatively charged actin residue D292 lying adjacent to residues K326, K328 and R147 is required to temper the binding of actin to tropomyosin allowing regulatory-switching.
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