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Open data
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Basic information
Entry | Database: PDB / ID: 4a7f | ||||||
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Title | Structure of the Actin-Tropomyosin-Myosin Complex (rigor ATM 3) | ||||||
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![]() | STRUCTURAL PROTEIN/HYDROLASE / STRUCTURAL PROTEIN-HYDROLASE COMPLEX / STRUCTURAL PROTEIN / CYTOSKELETON / CONTRACTILE FILAMENT / MOTOR ACTIVITY / MYOSIN BINDING / ACTIN BINDING / ATP CATABOLIC PROCESS / RIGOR STATE | ||||||
Function / homology | ![]() macropinocytic cup membrane / pseudopodium membrane / actin wave / macropinocytic cup cytoskeleton / chemotaxis to cAMP / macropinocytic cup / actin filament-based movement / leading edge membrane / early phagosome / myosin complex ...macropinocytic cup membrane / pseudopodium membrane / actin wave / macropinocytic cup cytoskeleton / chemotaxis to cAMP / macropinocytic cup / actin filament-based movement / leading edge membrane / early phagosome / myosin complex / cytoskeletal motor activator activity / microfilament motor activity / phagocytosis, engulfment / tropomyosin binding / mesenchyme migration / troponin I binding / myosin heavy chain binding / cell leading edge / pseudopodium / filamentous actin / actin filament bundle / phosphatidylinositol-3,4,5-trisphosphate binding / skeletal muscle thin filament assembly / striated muscle thin filament / actin filament bundle assembly / phagocytic cup / skeletal muscle myofibril / actin monomer binding / skeletal muscle fiber development / phagocytosis / muscle contraction / stress fiber / titin binding / actin filament polymerization / filopodium / actin filament organization / actin filament / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / endocytosis / calcium-dependent protein binding / actin filament binding / actin cytoskeleton / lamellipodium / actin binding / cell body / calmodulin binding / hydrolase activity / protein heterodimerization activity / protein domain specific binding / calcium ion binding / positive regulation of gene expression / magnesium ion binding / protein homodimerization activity / ATP binding / identical protein binding / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() ![]() | ||||||
Method | ELECTRON MICROSCOPY / helical reconstruction / cryo EM / Resolution: 7.7 Å | ||||||
![]() | Behrmann, E. / Mueller, M. / Penczek, P.A. / Mannherz, H.G. / Manstein, D.J. / Raunser, S. | ||||||
![]() | ![]() Title: Structure of the rigor actin-tropomyosin-myosin complex. Authors: Elmar Behrmann / Mirco Müller / Pawel A Penczek / Hans Georg Mannherz / Dietmar J Manstein / Stefan Raunser / ![]() Abstract: Regulation of myosin and filamentous actin interaction by tropomyosin is a central feature of contractile events in muscle and nonmuscle cells. However, little is known about molecular interactions ...Regulation of myosin and filamentous actin interaction by tropomyosin is a central feature of contractile events in muscle and nonmuscle cells. However, little is known about molecular interactions within the complex and the trajectory of tropomyosin movement between its "open" and "closed" positions on the actin filament. Here, we report the 8 Å resolution structure of the rigor (nucleotide-free) actin-tropomyosin-myosin complex determined by cryo-electron microscopy. The pseudoatomic model of the complex, obtained from fitting crystal structures into the map, defines the large interface involving two adjacent actin monomers and one tropomyosin pseudorepeat per myosin contact. Severe forms of hereditary myopathies are linked to mutations that critically perturb this interface. Myosin binding results in a 23 Å shift of tropomyosin along actin. Complex domain motions occur in myosin, but not in actin. Based on our results, we propose a structural model for the tropomyosin-dependent modulation of myosin binding to actin. | ||||||
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Structure visualization
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Structure viewer | Molecule: ![]() ![]() |
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PDBx/mmCIF format | ![]() | 764.3 KB | Display | ![]() |
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PDB format | ![]() | 631.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1987MC ![]() 1988C ![]() 1989C ![]() 1990C ![]() 4a7hC ![]() 4a7lC ![]() 4a7nC 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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Components
#1: Protein | Mass: 41875.633 Da / Num. of mol.: 5 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #2: Protein | Mass: 15807.628 Da / Num. of mol.: 2 / Fragment: RESIDUES 98-233 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #3: Protein | Mass: 79207.305 Da / Num. of mol.: 3 / Fragment: RESIDUES 1-697 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #4: Chemical | ChemComp-ADP / #5: Chemical | ChemComp-CA / Compound details | ENGINEERED RESIDUE IN CHAIN C, SER 334 TO GLU ENGINEERED RESIDUE IN CHAIN G, SER 334 TO GLU ...ENGINEERED | Sequence details | SEQUENCE AS DESCRIBED BY KOLLMAR, M., DURRWANG, U., KLICHE, W., MANSTEIN, D. J. & KULL, F. J. ...SEQUENCE AS DESCRIBED BY KOLLMAR, M., DURRWANG, U., KLICHE, W., MANSTEIN, D. J. & KULL, F. J. CRYSTAL STRUCTURE OF THE MOTOR DOMAIN OF A CLASS-I MYOSIN. EMBO J 21, 2517-2525, (2002) SEQUENCE IS NOT BASED ON THE EXPERIMENT | |
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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: COMPLEX OF F-ACTIN, MYOE AND TROPOMYOSIN / Type: COMPLEX / Details: CMOS IMAGE FRAMES SELECTED BY POWER SPECTRUM |
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Buffer solution | Name: 5 MM HEPES-OH, 100 MM KCL, 2 MM MGCL2, 50 MM GLUTAMINE, 50 MM ARGININE pH: 7.2 Details: 5 MM HEPES-OH, 100 MM KCL, 2 MM MGCL2, 50 MM GLUTAMINE, 50 MM ARGININE |
Specimen | Conc.: 0.01 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Specimen support | Details: HOLEY CARBON |
Vitrification | Instrument: GATAN CRYOPLUNGE 3 / Cryogen name: ETHANE / Details: LIQUID ETHANE |
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Electron microscopy imaging
Microscopy | Model: JEOL 3200FSC Details: BEST 836 MICROGRAPHS WERE SELECTED FROM OVER 3000 AQUIRED IMAGES |
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Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD / Nominal magnification: 80000 X / Calibrated magnification: 169644 X / Nominal defocus max: 1500 nm / Nominal defocus min: 750 nm / Cs: 4.1 mm |
Specimen holder | Temperature: 77 K |
Image recording | Electron dose: 1.7 e/Å2 / Film or detector model: TVIPS TEMCAM-F816 (8k x 8k) |
Image scans | Num. digital images: 836 |
Radiation wavelength | Relative weight: 1 |
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Processing
EM software |
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CTF correction | Details: INDIVIDUAL PARTICLES | ||||||||||||
3D reconstruction | Method: IHRSR / Resolution: 7.7 Å / Num. of particles: 5481 / Nominal pixel size: 1.84 Å / Actual pixel size: 1.84 Å Details: SUBMISSION BASED ON EXPERIMENTAL DATA FROM EMDB EMD-1987 DEPOSITION ID: 10340). Symmetry type: HELICAL | ||||||||||||
Atomic model building | Protocol: FLEXIBLE FIT / Space: REAL Details: METHOD--FLEXIBLE FITTING BY DEN REFINEMENT PROTOCOL--EM | ||||||||||||
Atomic model building |
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Refinement | Highest resolution: 7.7 Å | ||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 7.7 Å
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