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- PDB-7plz: 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: PDB / ID: 7plz | ||||||||||||||||||
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Title | Cryo-EM structure of the actomyosin-V complex in the rigor state (central 3er/2er, young JASP-stabilized F-actin) | ||||||||||||||||||
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![]() | MOTOR PROTEIN / myosin / cytoskeleton / F-actin / jasplakinolide | ||||||||||||||||||
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 | ELECTRON MICROSCOPY / helical reconstruction / cryo EM / Resolution: 3.2 Å | ||||||||||||||||||
![]() | Pospich, S. / Sweeney, H.L. / 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 | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 510.3 KB | Display | ![]() |
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PDB format | ![]() | 427.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 13507MC ![]() 7pltC ![]() 7pluC ![]() 7plvC ![]() 7plwC ![]() 7plxC ![]() 7plyC ![]() 7pm0C ![]() 7pm1C ![]() 7pm2C ![]() 7pm3C ![]() 7pm5C ![]() 7pm6C ![]() 7pm7C ![]() 7pm8C ![]() 7pm9C ![]() 7pmaC ![]() 7pmbC ![]() 7pmcC ![]() 7pmdC ![]() 7pmeC ![]() 7pmfC ![]() 7pmgC ![]() 7pmhC ![]() 7pmiC ![]() 7pmjC ![]() 7pmlC C: citing same article ( M: map data used to model this data |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Components
-Protein , 3 types, 7 molecules ADCFGBE
#1: Protein | Mass: 91363.953 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Protein | Mass: 42109.973 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #3: Protein | Mass: 17090.277 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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-Non-polymers , 4 types, 12 molecules ![](data/chem/img/ADP.gif)
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#4: Chemical | #5: Chemical | #6: Chemical | #7: Chemical | |
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-Details
Has ligand of interest | N |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: FILAMENT / 3D reconstruction method: helical reconstruction |
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Sample preparation
Component | Name: Young actomyosin-V complex in the rigor state / Type: COMPLEX Details: Young ADP-Pi-bound F-actin stabilized with jasplakinolide and decorated with myosin-Va-LC in the rigor state (nucleotide-free) Entity ID: #1-#3 / Source: MULTIPLE SOURCES |
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Molecular weight | Experimental value: NO |
Buffer solution | pH: 7.5 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES / Details: Rise 27.7 A, Twist -167.1 degrees |
Specimen support | Grid material: COPPER / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R2/1 |
Vitrification | Instrument: FEI VITROBOT MARK III / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 286 K / Details: On grid decoration |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD / Cs: 0 mm |
Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
Image recording | Average exposure time: 15 sec. / Electron dose: 80 e/Å2 / Detector mode: SUPER-RESOLUTION / Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Num. of grids imaged: 1 / Num. of real images: 3336 |
EM imaging optics | Energyfilter name: GIF Bioquantum / Energyfilter slit width: 20 eV / Spherical aberration corrector: Cs-corrected microscope |
Image scans | Movie frames/image: 40 |
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Processing
Software | Name: PHENIX / Version: 1.17.1_3660: / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||
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EM software |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||||||||||||||
3D reconstruction | Resolution: 3.2 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 414148 / Symmetry type: POINT | ||||||||||||||||||||||||||||||||||||||||
Atomic model building | Protocol: OTHER / Space: REAL Details: An initial model of jasplakinolide was generated using elBow within Phenix inputting the SMILES string. | ||||||||||||||||||||||||||||||||||||||||
Atomic model building | PDB-ID: 7PLY | ||||||||||||||||||||||||||||||||||||||||
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