|Entry||Database: EMDB / ID: 7029|
|Title||CryoEM map from poorly ordered myosin thick filaments isolated from asynchronous flight muscle of the large waterbug Lethocerus indicus|
|Map data||Primary map|
|Sample||Lethocerus flight muscle myosin filament:|
|Source||Lethocerus indicus (insect)|
|Method||single particle reconstruction / cryo EM / 6.4 Å resolution|
|Authors||Taylor KA / Taylor D / Hu Z / Edwards RJ|
|Citation||Journal: J. Struct. Biol. / Year: 2017|
Title: Coupling between myosin head conformation and the thick filament backbone structure.
Authors: Zhongjun Hu / Dianne W Taylor / Robert J Edwards / Kenneth A Taylor
Abstract: The recent high-resolution structure of the thick filament from Lethocerus asynchronous flight muscle shows aspects of thick filament structure never before revealed that may shed some light on how ...The recent high-resolution structure of the thick filament from Lethocerus asynchronous flight muscle shows aspects of thick filament structure never before revealed that may shed some light on how striated muscles function. The phenomenon of stretch activation underlies the function of asynchronous flight muscle. It is most highly developed in flight muscle, but is also observed in other striated muscles such as cardiac muscle. Although stretch activation is likely to be complex, involving more than a single structural aspect of striated muscle, the thick filament itself, would be a prime site for regulatory function because it must bear all of the tension produced by both its associated myosin motors and any externally applied force. Here we show the first structural evidence that the arrangement of myosin heads within the interacting heads motif is coupled to the structure of the thick filament backbone. We find that a change in helical angle of 0.16° disorders the blocked head preferentially within the Lethocerus interacting heads motif. This observation suggests a mechanism for how tension affects the dynamics of the myosin heads leading to a detailed hypothesis for stretch activation and shortening deactivation, in which the blocked head preferentially binds the thin filament followed by the free head when force production occurs.
|Date||Deposition: Sep 15, 2017 / Header (metadata) release: Oct 11, 2017 / Map release: Oct 11, 2017 / Last update: Feb 14, 2018|
|Structure viewer||EM map: |
Downloads & links
|File||emd_7029.map.gz (map file in CCP4 format, 322487 KB)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 1.223 Å|
CCP4 map header:
-Entire Lethocerus flight muscle myosin filament
|Entire||Name: Lethocerus flight muscle myosin filament / Number of components: 1|
-Component #1: protein, Lethocerus flight muscle myosin filament
|Protein||Name: Lethocerus flight muscle myosin filament / Recombinant expression: No|
|Source||Species: Lethocerus indicus (insect)|
|Source (natural)||Organelle: myofibril / Organ or tissue: striated muscle|
|Specimen||Specimen state: filament / Method: cryo EM|
|Sample solution||pH: 6.8|
|Support film||Gatan Solarus 950.M plasma cleaner|
|Vitrification||Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Temperature: 295 K / Humidity: 100 %|
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Imaging||Microscope: FEI TITAN KRIOS|
Details: All data collection details may be found in Z. Hu, D. W. Taylor, M. K. Reedy, R. J. Edwards, K. A. Taylor, Structure of myosin filaments from relaxed Lethocerus flight muscle by cryo-EM at 6 Angstrom resolution. Sci. Adv. 2, e1600058 (2016). Can also be found in the Specimen section of EMD-3301
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Electron dose: 65 e/Å2 / Illumination mode: FLOOD BEAM|
|Lens||Imaging mode: BRIGHT FIELD / Defocus: 1500 - 3000 nm|
|Specimen Holder||Model: FEI TITAN KRIOS AUTOGRID HOLDER|
|Image acquisition||Details: All specimen and sample preparation details may be found in Z. Hu, D. W. Taylor, M. K. Reedy, R. J. Edwards, K. A. Taylor, Structure of myosin filaments from relaxed Lethocerus flight muscle by cryo-EM at 6 Angstrom resolution. Sci. Adv. 2, e1600058 (2016). Can also be found in the Specimen section of EMD-3301|
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