|Entry||Database: PDB / ID: 7plv|
|Title||Cryo-EM structure of the actomyosin-V complex in the rigor state (central 1er, class 1)|
|Keywords||MOTOR PROTEIN / myosin / cytoskeleton / F-actin / phalloidin|
|Function / homology|
Function and homology information
minus-end directed microfilament motor activity / unconventional myosin complex / insulin-responsive compartment / muscle myosin complex / muscle filament sliding / myosin II complex / vesicle transport along actin filament / myosin complex / structural constituent of muscle / microfilament motor activity ...minus-end directed microfilament motor activity / unconventional myosin complex / insulin-responsive compartment / muscle myosin complex / muscle filament sliding / myosin II complex / vesicle transport along actin filament / myosin complex / structural constituent of muscle / microfilament motor activity / cytoskeletal motor activator activity / mesenchyme migration / tropomyosin binding / myosin heavy chain binding / troponin I binding / actin filament bundle / skeletal muscle thin filament assembly / filamentous actin / striated muscle thin filament / Smooth Muscle Contraction / actin filament bundle assembly / cytoskeletal motor activity / actin monomer binding / skeletal muscle myofibril / skeletal muscle fiber development / skeletal muscle tissue development / stress fiber / titin binding / actin filament polymerization / actin filament organization / muscle contraction / filopodium / vesicle-mediated transport / actin filament / protein localization to plasma membrane / cellular response to insulin stimulus / cell body / calcium-dependent protein binding / actin cytoskeleton / actin filament binding / lamellipodium / calmodulin binding / Golgi membrane / protein domain specific binding / calcium ion binding / positive regulation of gene expression / magnesium ion binding / extracellular exosome / ATP binding / identical protein binding / cytosol / cytoplasm
Similarity search - Function
Myosin 5a, cargo-binding domain / Class V myosin, motor domain / DIL domain / DIL / Dilute domain / Dilute domain profile. / IQ calmodulin-binding motif / Myosin, N-terminal, SH3-like / Myosin N-terminal SH3-like domain profile. / Short calmodulin-binding motif containing conserved Ile and Gln residues. ...Myosin 5a, cargo-binding domain / Class V myosin, motor domain / DIL domain / DIL / Dilute domain / Dilute domain profile. / IQ calmodulin-binding motif / Myosin, N-terminal, SH3-like / Myosin N-terminal SH3-like domain profile. / Short calmodulin-binding motif containing conserved Ile and Gln residues. / Myosin head (motor domain) / Myosin motor domain profile. / Myosin. Large ATPases. / Myosin head, motor domain / IQ motif profile. / IQ motif, EF-hand binding site / Actins signature 1. / Actins signature 2. / Actin, conserved site / Actin/actin-like conserved site / Actins and actin-related proteins signature. / Actin / Actin family / Actin / Kinesin motor domain superfamily / ATPase, nucleotide binding domain / EF-hand, calcium binding motif / EF-hand calcium-binding domain profile. / EF-hand domain / EF-hand domain pair / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Actin, alpha skeletal muscle / : / Myosin light chain 6B / ADENOSINE-5'-DIPHOSPHATE / Unconventional myosin-Va
Similarity search - Component
|Biological species||Homo sapiens (human)|
Gallus gallus (chicken)
Oryctolagus cuniculus (rabbit)
synthetic construct (others)
|Method||ELECTRON MICROSCOPY / helical reconstruction / cryo EM / Resolution: 3.5 Å|
|Authors||Pospich, S. / Sweeney, H.L. / Houdusse, A. / Raunser, S.|
|Funding support|| Germany, European Union, France, United States, 5items |
|Citation||Journal: Elife / Year: 2021|
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.
|Structure viewer||Molecule: |
Downloads & links
B: Myosin light chain 6B
A: Unconventional myosin-Va
C: Actin, alpha skeletal muscle
-Protein , 3 types, 3 molecules B
|#1: Protein|| |
Mass: 17090.277 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: MYL6B, MLC1SA / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: P14649
|#2: Protein|| |
Mass: 91363.953 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Gallus gallus (chicken) / Gene: MYO5A / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: Q02440
|#3: Protein|| |
Mass: 42109.973 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Oryctolagus cuniculus (rabbit) / References: UniProt: P68135
-Protein/peptide , 1 types, 1 molecules H
|#4: Protein/peptide|| |
Type: Peptide-like / Class: Toxin / Mass: 808.899 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: From Amanita phalloides, Tax id 67723 / Source: (synth.) synthetic construct (others) / References: BIRD: PRD_002366
-Non-polymers , 2 types, 2 molecules
|#5: Chemical|| ChemComp-ADP / |
|#6: Chemical|| ChemComp-MG / |
|Has ligand of interest||N|
|Experiment||Method: ELECTRON MICROSCOPY|
|EM experiment||Aggregation state: FILAMENT / 3D reconstruction method: helical reconstruction|
|Molecular weight||Experimental value: NO|
|Buffer solution||pH: 7.5|
|Specimen||Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES / Details: Signal subtracted|
|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|
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Microscopy||Model: FEI TITAN KRIOS|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: SPOT SCAN|
|Electron lens||Mode: BRIGHT FIELDBright-field microscopy / Cs: 2.7 mm|
|Specimen holder||Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER|
|Image recording||Average exposure time: 15 sec. / Electron dose: 79 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: 3623|
|EM imaging optics||Energyfilter name: GIF Bioquantum / Energyfilter slit width: 20 eV|
|Image scans||Movie frames/image: 40|
|Software||Name: PHENIX / Version: 1.17.1_3660: / Classification: refinement|
|CTF correction||Type: PHASE FLIPPING AND AMPLITUDE CORRECTION|
|Helical symmerty||Angular rotation/subunit: -167.3 ° / Axial rise/subunit: 27.8 Å / Axial symmetry: C1|
|3D reconstruction||Resolution: 3.5 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 94077 / Num. of class averages: 1 / Symmetry type: POINT|
|Atomic model building||Protocol: OTHER / Space: REAL|
Details: Starting from average model and ChimeraX-Isolde session
|Atomic model building||PDB-ID: 7PLT|
|Refine LS restraints|
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