Visualization of an unstable coiled coil from the scallop myosin rod

Yu Li, Jerry H. Brown, Ludmilla Reshetnikova, Antal Blazsek, László Farkas, László Nyitray and Carolyn Cohen ()
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Yu Li: Brandeis University
Jerry H. Brown: Brandeis University
Ludmilla Reshetnikova: Brandeis University
Antal Blazsek: Eötvös Loránd University
László Farkas: Eötvös Loránd University
László Nyitray: Eötvös Loránd University
Carolyn Cohen: Brandeis University

Nature, 2003, vol. 424, issue 6946, 341-345

Abstract: Abstract 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.

Date: 2003
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DOI: 10.1038/nature01801

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