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TitleCryoEM structure of flight muscle thick filaments at 7 Å resolution.
Journal, issue, pagesLife Sci Alliance, Vol. 3, Issue 8, Year 2020
Publish dateJul 27, 2020
AuthorsNadia Daneshparvar / Dianne W Taylor / Thomas S O'Leary / Hamidreza Rahmani / Fatemeh Abbasiyeganeh / Michael J Previs / Kenneth A Taylor /
PubMed AbstractStriated 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- ...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 at 7 Å resolution. Its myosin tails are arranged in curved molecular crystalline layers identical to flight muscles of the giant water bug Four non-myosin densities are observed, three of which correspond to ones found in ; 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.
External linksLife Sci Alliance / PubMed:32718994 / PubMed Central
MethodsEM (single particle)
Resolution7.0 - 8.0 Å
Structure data

EMDB-22217:
Drosophila Flight Muscle Thick Filament
Method: EM (single particle) / Resolution: 7.0 Å

EMDB-22218:
Drosophila Dmlc2[2-46; S66A,S67A] mutant
Method: EM (single particle) / Resolution: 8.0 Å

Source
  • Drosophila melanogaster (fruit fly)

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