- EMDB-28081: Human beta-cardiac myosin II bound to ADP-MG2+ and the associated... -
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Basic information
Entry
Database: EMDB / ID: EMD-28081
Title
Human beta-cardiac myosin II bound to ADP-MG2+ and the associated essential light chain
Map data
Primary map for the single particle structure of the human cardiac beta-myosin II bound to ADP-Mg2 on actin.
Sample
Complex: Complex of the human beta cardiac myosin II bound to ADP-Mg2+ with the associated essential light chain.
Complex: Human beta-cardiac myosin II
Protein or peptide: Beta-cardiac myosin II
Complex: Mouse skeletal essential light chain
Protein or peptide: Myosin light chain 1/3, skeletal muscle isoform
Ligand: MAGNESIUM ION
Ligand: ADENOSINE-5'-DIPHOSPHATE
Keywords
actin / tropomyosin / myosin / cardiac / CONTRACTILE PROTEIN
Function / homology
Function and homology information
regulation of slow-twitch skeletal muscle fiber contraction / Striated Muscle Contraction / regulation of the force of skeletal muscle contraction / muscle myosin complex / muscle filament sliding / regulation of the force of heart contraction / transition between fast and slow fiber / myosin filament / adult heart development / cardiac muscle hypertrophy in response to stress ...regulation of slow-twitch skeletal muscle fiber contraction / Striated Muscle Contraction / regulation of the force of skeletal muscle contraction / muscle myosin complex / muscle filament sliding / regulation of the force of heart contraction / transition between fast and slow fiber / myosin filament / adult heart development / cardiac muscle hypertrophy in response to stress / myosin II complex / myosin complex / structural constituent of muscle / ventricular cardiac muscle tissue morphogenesis / sarcomere organization / microfilament motor activity / myofibril / skeletal muscle contraction / ATP metabolic process / striated muscle contraction / stress fiber / cardiac muscle contraction / muscle contraction / regulation of heart rate / sarcomere / Z disc / actin filament binding / calmodulin binding / calcium ion binding / ATP binding / cytoplasm Similarity search - Function
DNA repair protein XRCC4-like, C-terminal / Myosin tail / Myosin tail / Myosin N-terminal SH3-like domain / Myosin S1 fragment, N-terminal / Myosin, N-terminal, SH3-like / Myosin N-terminal SH3-like domain profile. / Short calmodulin-binding motif containing conserved Ile and Gln residues. / IQ motif, EF-hand binding site / Myosin head, motor domain ...DNA repair protein XRCC4-like, C-terminal / Myosin tail / Myosin tail / Myosin N-terminal SH3-like domain / Myosin S1 fragment, N-terminal / Myosin, N-terminal, SH3-like / Myosin N-terminal SH3-like domain profile. / Short calmodulin-binding motif containing conserved Ile and Gln residues. / IQ motif, EF-hand binding site / Myosin head, motor domain / Myosin head (motor domain) / Myosin motor domain profile. / Myosin. Large ATPases. / IQ motif profile. / : / Kinesin motor domain superfamily / EF-hand calcium-binding domain profile. / EF-hand domain / EF-hand domain pair / P-loop containing nucleoside triphosphate hydrolase Similarity search - Domain/homology
National Institutes of Health/National Heart, Lung, and Blood Institute (NIH/NHLBI)
R01HL036153
United States
Citation
Journal: J Gen Physiol / Year: 2023 Title: Conformational changes linked to ADP release from human cardiac myosin bound to actin-tropomyosin. Authors: Matthew H Doran / Michael J Rynkiewicz / David Rasicci / Skylar M L Bodt / Meaghan E Barry / Esther Bullitt / Christopher M Yengo / Jeffrey R Moore / William Lehman / Abstract: Following binding to the thin filament, β-cardiac myosin couples ATP-hydrolysis to conformational rearrangements in the myosin motor that drive myofilament sliding and cardiac ventricular ...Following binding to the thin filament, β-cardiac myosin couples ATP-hydrolysis to conformational rearrangements in the myosin motor that drive myofilament sliding and cardiac ventricular contraction. However, key features of the cardiac-specific actin-myosin interaction remain uncertain, including the structural effect of ADP release from myosin, which is rate-limiting during force generation. In fact, ADP release slows under experimental load or in the intact heart due to the afterload, thereby adjusting cardiac muscle power output to meet physiological demands. To further elucidate the structural basis of this fundamental process, we used a combination of cryo-EM reconstruction methodologies to determine structures of the human cardiac actin-myosin-tropomyosin filament complex at better than 3.4 Å-resolution in the presence and in the absence of Mg2+·ADP. Focused refinements of the myosin motor head and its essential light chains in these reconstructions reveal that small changes in the nucleotide-binding site are coupled to significant rigid body movements of the myosin converter domain and a 16-degree lever arm swing. Our structures provide a mechanistic framework to understand the effect of ADP binding and release on human cardiac β-myosin, and offer insights into the force-sensing mechanism displayed by the cardiac myosin motor.
Entire : Complex of the human beta cardiac myosin II bound to ADP-Mg2+ wit...
Entire
Name: Complex of the human beta cardiac myosin II bound to ADP-Mg2+ with the associated essential light chain.
Components
Complex: Complex of the human beta cardiac myosin II bound to ADP-Mg2+ with the associated essential light chain.
Complex: Human beta-cardiac myosin II
Protein or peptide: Beta-cardiac myosin II
Complex: Mouse skeletal essential light chain
Protein or peptide: Myosin light chain 1/3, skeletal muscle isoform
Ligand: MAGNESIUM ION
Ligand: ADENOSINE-5'-DIPHOSPHATE
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Supramolecule #1: Complex of the human beta cardiac myosin II bound to ADP-Mg2+ wit...
Supramolecule
Name: Complex of the human beta cardiac myosin II bound to ADP-Mg2+ with the associated essential light chain. type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2
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Supramolecule #2: Human beta-cardiac myosin II
Supramolecule
Name: Human beta-cardiac myosin II / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1
Name: Myosin light chain 1/3, skeletal muscle isoform / type: protein_or_peptide / ID: 2 Details: Mouse skeletal muscle essential light chain 1/3 that was purified with the human cardiac myosin II. Number of copies: 1 / Enantiomer: LEVO
Model: Quantifoil R1.2/1.3 / Material: GOLD / Mesh: 400 / Support film - Material: GOLD / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 30 sec. Details: 15 mA was used in the Pelco Easiglow glow discharge machine
Vitrification
Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 283 K / Instrument: FEI VITROBOT MARK III
Details
This complex was part of a larger filament containing actin-tropomyosin. The map was a result of a focused single particle approach.
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Electron microscopy
Microscope
FEI TITAN KRIOS
Specialist optics
Energy filter - Name: In-column Omega Filter / Energy filter - Slit width: 20 eV
Image recording
Film or detector model: GATAN K3 (6k x 4k) / Detector mode: COUNTING / Digitization - Frames/image: 1-35 / Number grids imaged: 4 / Number real images: 3961 / Average exposure time: 3.12 sec. / Average electron dose: 53.7 e/Å2
Electron beam
Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
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