CryoEM structure of<i>Drosophila</i>flight muscle thick filaments at 7 Å resolution
Nadia Daneshparvar, Dianne W. Taylor, Thomas S. O’Leary, Hamidreza Rahmani, Fatemeh Abbasi Yeganeh, Michael J. Previs, Kenneth A. Taylor
Abstract
Striated muscle thick filaments are composed of myosin II and several non-myosin proteins. Myosin II’s long α-helical coiled-coil tail forms the dense protein backbone of filaments, whereas its N-terminal globular head containing the catalytic and actin-binding activities extends outward from the backbone. Here, we report the structure of thick filaments of the flight muscle of the fruit fly Drosophila melanogaster at 7 Å resolution. Its myosin tails are arranged in curved molecular crystalline layers identical to flight muscles of the giant water bug Lethocerus indicus . Four non-myosin densities are observed, three of which correspond to ones found in Lethocerus ; one new density, possibly stretchin-mlck, is found on the backbone outer surface. Surprisingly, the myosin heads are disordered rather than ordered along the filament backbone. Our results show striking myosin tail similarity within flight muscle filaments of two insect orders separated by several hundred million years of evolution.