Visualization of an unstable coiled coil from the scallop myosin rod

α-Helical coiled coils in muscle exemplify simplicity and economy of protein design: small variations in sequence lead to remarkable diversity in cellular functions1,2. Myosin II is the key protein in muscle contraction, and the molecule's two-chain α-helical coiled-coil rod region—towards the carboxy terminus of the heavy chain—has unusual structural and dynamic features. The amino-terminal subfragment-2 (S2) domains of the rods can swing out from the thick filament backbone at a hinge in the coiled coil, allowing the two myosin ‘heads’ and their motor domains to interact with actin and generate tension3. Most of the S2 rod appears to be a flexible coiled coil, but studies suggest that the structure at the N-terminal region is unstable4,5,6, and unwinding or bending of the α-helices near the head–rod junction seems necessary for many of myosin's functional properties7,8. Here we show the physical basis of a particularly weak coiled-coil segment by determining the 2.5-Å-resolution crystal structure of a leucine-zipper-stabilized fragment of the scallop striated-muscle myosin rod adjacent to the head–rod junction. The N-terminal 14 residues are poorly ordered; the rest of the S2 segment forms a flexible coiled coil with poorly packed core residues. The unusual absence of interhelical salt bridges here exposes apolar core atoms to solvent.