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- W2912089482 abstract "The structure of muscle thick filaments is essential to muscle physiology and understanding different inherited myopathies. Recently, the relaxed thick filament structure from the large waterbug Lethocerus indicus was reported at a resolution of 5.5 Å confirming a model for myosin rods packing into ribbons and observing four non-myosin densities “threaded” among the myosin rods. A larger data set taken on the DE64 detector, as well as novel efforts on sample preparations and data analysis have led to a new structure of with the resolution of 4.1 Å in the backbone. Although we cannot resolve every single side-chain and the alpha-helix completely, sharpening tools like local deblur have helped us locating most of the larger side chains. We used these side chains as guides to manually build an atomic structure without using any coiled-coil constraints, unlike the previous model. This is the first atomic structure of the complete myosin molecule in its native structure, resolved thanks to the helical symmetry of thick filaments in insect flight muscle. After building this model, we placed myosin molecules back in the structure to be able to look at their interactions, specifically the known mutations on the preserved sites between Lethocerus and Human cardiac myosin. Lethocerus flight muscle myosin II and human beta-cardiac myosin have substantial similarities both in sequence and arrangement. Even though our model needs additional refinements, we looked at ∼200 mutation sites (∼150 preserved) in the myosin backbone and observed that ∼40 relate to coiled-coil interaction and ∼50 mutations happen where two myosin molecules are interacting, and both sites are preserved. Therefore, a complete structure of the Lethocerus myosin filament can entail substantial information relevant to the cardiomyopathy mutations. Supported by NIH." @default.
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- W2912089482 date "2019-02-01" @default.
- W2912089482 modified "2023-10-18" @default.
- W2912089482 title "A Complete Atomic Model for Lethocerus Flight Muscle Myosin Filament" @default.
- W2912089482 doi "https://doi.org/10.1016/j.bpj.2018.11.888" @default.
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