|Entry||Database: PDB / ID: 6z47|
|Title||Smooth muscle myosin shutdown state heads region|
|Keywords||CONTRACTILE PROTEIN / myosin / motor / inhibited state / shutdown state / smooth muscle|
|Function / homology|
Function and homology information
myosin complex / cytoskeletal motor activity / actin filament binding / calcium ion binding / ATP binding / cytosol
Similarity search - Function
EF-hand domain / DNA repair protein XRCC4-like, C-terminal / Myosin tail / Myosin N-terminal SH3-like domain / Myosin tail / Myosin S1 fragment, N-terminal / EF-hand domain pair / Myosin, N-terminal, SH3-like / Myosin N-terminal SH3-like domain profile. / Short calmodulin-binding motif containing conserved Ile and Gln residues. ...EF-hand domain / DNA repair protein XRCC4-like, C-terminal / Myosin tail / Myosin N-terminal SH3-like domain / Myosin tail / Myosin S1 fragment, N-terminal / EF-hand domain pair / Myosin, N-terminal, SH3-like / Myosin N-terminal SH3-like domain profile. / Short calmodulin-binding motif containing conserved Ile and Gln residues. / Myosin. Large ATPases. / Myosin head, motor domain / Myosin head (motor domain) / Myosin motor domain profile. / IQ motif profile. / IQ motif, EF-hand binding site / Kinesin motor domain superfamily / EF-hand, calcium binding motif / EF-Hand 1, calcium-binding site / EF-hand calcium-binding domain. / EF-hand calcium-binding domain profile. / EF-hand domain / EF-hand domain pair / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Uncharacterized protein / ADENOSINE-5'-DIPHOSPHATE / Uncharacterized protein / PHOSPHATE ION / Myosin light chain smooth muscle isoform
Similarity search - Component
|Biological species||Meleagris gallopavo (turkey)|
|Method||ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 6.3 Å|
|Authors||Scarff, C.A. / Carrington, G. / Casas Mao, D. / Chalovich, J.M. / Knight, P.J. / Ranson, N.A. / Peckham, M.|
|Funding support|| United Kingdom, 3items |
|Citation||Journal: Nature / Year: 2020|
Title: Structure of the shutdown state of myosin-2.
Authors: Charlotte A Scarff / Glenn Carrington / David Casas-Mao / Joseph M Chalovich / Peter J Knight / Neil A Ranson / Michelle Peckham /
Abstract: Myosin-2 is essential for processes as diverse as cell division and muscle contraction. Dephosphorylation of its regulatory light chain promotes an inactive, 'shutdown' state with the filament- ...Myosin-2 is essential for processes as diverse as cell division and muscle contraction. Dephosphorylation of its regulatory light chain promotes an inactive, 'shutdown' state with the filament-forming tail folded onto the two heads, which prevents filament formation and inactivates the motors. The mechanism by which this happens is unclear. Here we report a cryo-electron microscopy structure of shutdown smooth muscle myosin with a resolution of 6 Å in the head region. A pseudo-atomic model, obtained by flexible fitting of crystal structures into the density and molecular dynamics simulations, describes interaction interfaces at the atomic level. The N-terminal extension of one regulatory light chain interacts with the tail, and the other with the partner head, revealing how the regulatory light chains stabilize the shutdown state in different ways and how their phosphorylation would allow myosin activation. Additional interactions between the three segments of the coiled coil, the motor domains and the light chains stabilize the shutdown molecule. The structure of the lever in each head is competent to generate force upon activation. This shutdown structure is relevant to all isoforms of myosin-2 and provides a framework for understanding their disease-causing mutations.
|Structure viewer||Molecule: |
Downloads & links
A: Myosin heavy chain 11
B: Myosin heavy chain 11
C: Myosin light chain smooth muscle isoform
D: Myosin light chain smooth muscle isoform
E: Myosin light chain 9
F: Myosin light chain 9
G: Myosin heavy chain 11
H: Myosin heavy chain 11
-Myosin light chain ... , 2 types, 4 molecules C
D E F
Mass: 16989.145 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Meleagris gallopavo (turkey) / References: UniProt: Q6W5H0
Mass: 19872.244 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Meleagris gallopavo (turkey) / References: UniProt: G3URE9
-Antibody , 1 types, 4 molecules A
B G H
Mass: 229148.250 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Meleagris gallopavo (turkey) / Tissue: Gizzard / References: UniProt: G1N5L2
-Non-polymers , 3 types, 8 molecules
Mass: 427.201 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H15N5O10P2 / Comment: ADP, energy-carrying molecule*YM
|Has ligand of interest||N|
|Experiment||Method: ELECTRON MICROSCOPY|
|EM experiment||Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction|
|Component||Name: Smooth muscle myosin in the shutdown state / Type: COMPLEX / Entity ID: #1-#3 / Source: NATURAL|
|Molecular weight||Experimental value: NO|
|Source (natural)||Organism: Meleagris gallopavo (turkey)|
|Buffer solution||pH: 7.2|
|Specimen||Conc.: 0.45 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES|
Details: Smooth muscle myosin from turkey gizzard, stored under liquid nitrogen, was thawed quickly. MgATP was added before dilution into the final buffer conditions stated below
|Specimen support||Details: GloCube / Grid material: COPPER / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R2/1|
|Vitrification||Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 281 K / Details: Blot force 6, blot time 3 seconds|
-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: FLOOD BEAM|
|Electron lens||Mode: BRIGHT FIELDBright-field microscopy|
|Specimen holder||Model: FEI TITAN KRIOS AUTOGRID HOLDER|
|Image recording||Electron dose: 60 e/Å2 / Detector mode: COUNTING / Film or detector model: GATAN K2 QUANTUM (4k x 4k)|
|CTF correction||Type: PHASE FLIPPING AND AMPLITUDE CORRECTION|
|Symmetry||Point symmetry: C1 (asymmetric)|
|3D reconstruction||Resolution: 6.3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 96351 / Symmetry type: POINT|
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