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- EMDB-13504: Cryo-EM structure of the actomyosin-V complex in the rigor state ... -
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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-13504 | ||||||||||||||||||
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Title | Cryo-EM structure of the actomyosin-V complex in the rigor state (central 1er, class 2) | ||||||||||||||||||
![]() | Sharpened map of the central actomyosin-V-LC molecule filtered to local resolution (class 2) | ||||||||||||||||||
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Function / homology | ![]() minus-end directed microfilament motor activity / unconventional myosin complex / insulin-responsive compartment / vesicle transport along actin filament / muscle myosin complex / muscle filament sliding / myosin II complex / myosin complex / structural constituent of muscle / cytoskeletal motor activator activity ...minus-end directed microfilament motor activity / unconventional myosin complex / insulin-responsive compartment / vesicle transport along actin filament / muscle myosin complex / muscle filament sliding / myosin II complex / myosin complex / structural constituent of muscle / cytoskeletal motor activator activity / microfilament motor activity / tropomyosin binding / mesenchyme migration / troponin I binding / myosin heavy chain binding / filamentous actin / actin filament bundle / cytoskeletal motor activity / skeletal muscle thin filament assembly / striated muscle thin filament / actin filament bundle assembly / skeletal muscle myofibril / actin monomer binding / Smooth Muscle Contraction / skeletal muscle fiber development / muscle contraction / stress fiber / skeletal muscle tissue development / titin binding / vesicle-mediated transport / actin filament polymerization / filopodium / actin filament organization / protein localization to plasma membrane / actin filament / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / cellular response to insulin stimulus / actin filament binding / calcium-dependent protein binding / actin cytoskeleton / lamellipodium / cell body / vesicle / calmodulin binding / hydrolase activity / protein domain specific binding / Golgi membrane / calcium ion binding / positive regulation of gene expression / magnesium ion binding / extracellular exosome / ATP binding / identical protein binding / membrane / cytoplasm / cytosol Similarity search - Function | ||||||||||||||||||
Biological species | ![]() ![]() ![]() ![]() ![]() ![]() ![]() | ||||||||||||||||||
Method | helical reconstruction / cryo EM / Resolution: 3.5 Å | ||||||||||||||||||
![]() | Pospich S / Sweeney HL / Houdusse A / Raunser S | ||||||||||||||||||
Funding support | ![]() ![]() ![]()
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![]() | ![]() Title: High-resolution structures of the actomyosin-V complex in three nucleotide states provide insights into the force generation mechanism. Authors: Sabrina Pospich / H Lee Sweeney / Anne Houdusse / Stefan Raunser / ![]() ![]() ![]() Abstract: The molecular motor myosin undergoes a series of major structural transitions during its force-producing motor cycle. The underlying mechanism and its coupling to ATP hydrolysis and actin binding are ...The molecular motor myosin undergoes a series of major structural transitions during its force-producing motor cycle. The underlying mechanism and its coupling to ATP hydrolysis and actin binding are only partially understood, mostly due to sparse structural data on actin-bound states of myosin. Here, we report 26 high-resolution cryo-EM structures of the actomyosin-V complex in the strong-ADP, rigor, and a previously unseen post-rigor transition state that binds the ATP analog AppNHp. The structures reveal a high flexibility of myosin in each state and provide valuable insights into the structural transitions of myosin-V upon ADP release and binding of AppNHp, as well as the actomyosin interface. In addition, they show how myosin is able to specifically alter the structure of F-actin. | ||||||||||||||||||
History |
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Structure visualization
Movie |
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Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 1.4 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 29.3 KB 29.3 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 11.7 KB | Display | ![]() |
Images | ![]() | 96.6 KB | ||
Masks | ![]() | 125 MB | ![]() | |
Others | ![]() ![]() ![]() ![]() | 1.5 MB 12.1 MB 59.5 MB 59.6 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7plwMC ![]() 7pltC ![]() 7pluC ![]() 7plvC ![]() 7plxC ![]() 7plyC ![]() 7plzC ![]() 7pm0C ![]() 7pm1C ![]() 7pm2C ![]() 7pm3C ![]() 7pm5C ![]() 7pm6C ![]() 7pm7C ![]() 7pm8C ![]() 7pm9C ![]() 7pmaC ![]() 7pmbC ![]() 7pmcC ![]() 7pmdC ![]() 7pmeC ![]() 7pmfC ![]() 7pmgC ![]() 7pmhC ![]() 7pmiC ![]() 7pmjC ![]() 7pmlC M: atomic model generated by this map C: citing same article ( |
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Similar structure data |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Annotation | Sharpened map of the central actomyosin-V-LC molecule filtered to local resolution (class 2) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.06 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Mask #1
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Projections & Slices |
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Density Histograms |
-Additional map: Sharpened map of the central actomyosin-V-LC molecule filtered...
File | emd_13504_additional_1.map | ||||||||||||
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Annotation | Sharpened map of the central actomyosin-V-LC molecule filtered to nominal resolution (class 2) | ||||||||||||
Projections & Slices |
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Density Histograms |
-Additional map: Denoised map of the central actomyosin-V-LC molecule (LAFTER,...
File | emd_13504_additional_2.map | ||||||||||||
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Annotation | Denoised map of the central actomyosin-V-LC molecule (LAFTER, class 2) | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Half map (signal subtracted particles, class 2)
File | emd_13504_half_map_1.map | ||||||||||||
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Annotation | Half map (signal subtracted particles, class 2) | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Half map (signal subtracted particles, class 2)
File | emd_13504_half_map_2.map | ||||||||||||
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Annotation | Half map (signal subtracted particles, class 2) | ||||||||||||
Projections & Slices |
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Density Histograms |
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Sample components
+Entire : Actomyosin-V complex in the rigor state
+Supramolecule #1: Actomyosin-V complex in the rigor state
+Supramolecule #2: Myosin light chain 6B
+Supramolecule #3: Unconventional myosin-Va
+Supramolecule #4: Actin, alpha skeletal muscle
+Supramolecule #5: Phalloidin
+Macromolecule #1: Myosin light chain 6B
+Macromolecule #2: Unconventional myosin-Va
+Macromolecule #3: Actin, alpha skeletal muscle
+Macromolecule #4: Phalloidin
+Macromolecule #5: ADENOSINE-5'-DIPHOSPHATE
+Macromolecule #6: MAGNESIUM ION
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | helical reconstruction |
Aggregation state | filament |
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Sample preparation
Buffer | pH: 7.5 |
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Grid | Model: Quantifoil R2/1 / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 286 K / Instrument: FEI VITROBOT MARK III / Details: On grid decoration. |
Details | Signal subtracted |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Specialist optics | Energy filter - Name: GIF Bioquantum / Energy filter - Slit width: 20 eV |
Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: SUPER-RESOLUTION / Number grids imaged: 1 / Number real images: 3623 / Average exposure time: 15.0 sec. / Average electron dose: 79.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |