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Yorodumi- PDB-6cxj: Cardiac thin filament decorated with C0C1 fragment of cardiac myo... -
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-Basic information
Entry | Database: PDB / ID: 6cxj | ||||||
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Title | Cardiac thin filament decorated with C0C1 fragment of cardiac myosin binding protein C mode 2 | ||||||
Components |
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Keywords | MOTOR PROTEIN / myosin binding protein C | ||||||
Function / homology | Function and homology information basal body patch / C zone / regulation of muscle filament sliding / striated muscle myosin thick filament / tight junction assembly / cardiac myofibril / regulation of transepithelial transport / structural constituent of postsynaptic actin cytoskeleton / regulation of striated muscle contraction / morphogenesis of a polarized epithelium ...basal body patch / C zone / regulation of muscle filament sliding / striated muscle myosin thick filament / tight junction assembly / cardiac myofibril / regulation of transepithelial transport / structural constituent of postsynaptic actin cytoskeleton / regulation of striated muscle contraction / morphogenesis of a polarized epithelium / protein localization to bicellular tight junction / profilin binding / Formation of annular gap junctions / Gap junction degradation / dense body / Cell-extracellular matrix interactions / Adherens junctions interactions / Striated Muscle Contraction / regulation of stress fiber assembly / positive regulation of ATP-dependent activity / Sensory processing of sound by inner hair cells of the cochlea / Sensory processing of sound by outer hair cells of the cochlea / Interaction between L1 and Ankyrins / A band / structural constituent of muscle / NuA4 histone acetyltransferase complex / sarcomere organization / regulation of synaptic vesicle endocytosis / apical junction complex / ventricular cardiac muscle tissue morphogenesis / maintenance of blood-brain barrier / regulation of focal adhesion assembly / myosin binding / positive regulation of wound healing / myosin heavy chain binding / myofibril / Recycling pathway of L1 / filamentous actin / ATPase activator activity / calyx of Held / EPH-ephrin mediated repulsion of cells / RHO GTPases Activate WASPs and WAVEs / RHO GTPases activate IQGAPs / RHOBTB2 GTPase cycle / phagocytic vesicle / heart morphogenesis / titin binding / cardiac muscle contraction / EPHB-mediated forward signaling / sarcomere / axonogenesis / cell motility / actin filament / Translocation of SLC2A4 (GLUT4) to the plasma membrane / RHO GTPases Activate Formins / FCGR3A-mediated phagocytosis / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / Signaling by high-kinase activity BRAF mutants / Schaffer collateral - CA1 synapse / MAP2K and MAPK activation / structural constituent of cytoskeleton / cellular response to type II interferon / Regulation of actin dynamics for phagocytic cup formation / platelet aggregation / VEGFA-VEGFR2 Pathway / Signaling by RAF1 mutants / Signaling by moderate kinase activity BRAF mutants / Paradoxical activation of RAF signaling by kinase inactive BRAF / Signaling downstream of RAS mutants / cell-cell junction / Signaling by BRAF and RAF1 fusions / Clathrin-mediated endocytosis / actin binding / angiogenesis / blood microparticle / cytoskeleton / hydrolase activity / cell adhesion / positive regulation of cell migration / axon / focal adhesion / synapse / ubiquitin protein ligase binding / positive regulation of gene expression / protein kinase binding / extracellular space / extracellular exosome / ATP binding / membrane / metal ion binding / nucleus / identical protein binding / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | ELECTRON MICROSCOPY / helical reconstruction / cryo EM / Resolution: 11 Å | ||||||
Authors | Galkin, V.E. / Schroeder, G.F. | ||||||
Funding support | United States, 1items
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Citation | Journal: Structure / Year: 2018 Title: N-Terminal Domains of Cardiac Myosin Binding Protein C Cooperatively Activate the Thin Filament. Authors: Cristina Risi / Betty Belknap / Eva Forgacs-Lonart / Samantha P Harris / Gunnar F Schröder / Howard D White / Vitold E Galkin / Abstract: Muscle contraction relies on interaction between myosin-based thick filaments and actin-based thin filaments. Myosin binding protein C (MyBP-C) is a key regulator of actomyosin interactions. Recent ...Muscle contraction relies on interaction between myosin-based thick filaments and actin-based thin filaments. Myosin binding protein C (MyBP-C) is a key regulator of actomyosin interactions. Recent studies established that the N'-terminal domains (NTDs) of MyBP-C can either activate or inhibit thin filaments, but the mechanism of their collective action is poorly understood. Cardiac MyBP-C (cMyBP-C) harbors an extra NTD, which is absent in skeletal isoforms of MyBP-C, and its role in regulation of cardiac contraction is unknown. Here we show that the first two domains of human cMyPB-C (i.e., C0 and C1) cooperate to activate the thin filament. We demonstrate that C1 interacts with tropomyosin via a positively charged loop and that this interaction, stabilized by the C0 domain, is required for thin filament activation by cMyBP-C. Our data reveal a mechanism by which cMyBP-C can modulate cardiac contraction and demonstrate a function of the C0 domain. | ||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | Molecule: MolmilJmol/JSmol |
-Downloads & links
-Download
PDBx/mmCIF format | 6cxj.cif.gz | 534.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6cxj.ent.gz | 427.9 KB | Display | PDB format |
PDBx/mmJSON format | 6cxj.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cx/6cxj ftp://data.pdbj.org/pub/pdb/validation_reports/cx/6cxj | HTTPS FTP |
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-Related structure data
Related structure data | 7781MC 4346C 7780C 6cxiC 6g2tC M: map data used to model this data C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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-Components
#1: Protein | Mass: 41838.766 Da / Num. of mol.: 5 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ACTG1, ACTG / Production host: Homo sapiens (human) / References: UniProt: P63261 #2: Protein | Mass: 12180.806 Da / Num. of mol.: 6 / Fragment: C1 Ig-domain (UNP residues 151-258) Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: MYBPC3 / Production host: Escherichia coli (E. coli) / References: UniProt: Q14896 #3: Protein | Mass: 10706.060 Da / Num. of mol.: 5 / Fragment: C0 Ig-domain (UNP residues 1-101) Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: MYBPC3 / Production host: Escherichia coli (E. coli) / References: UniProt: Q14896 #4: Protein | Mass: 10826.337 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Details: model / Source: (gene. exp.) Homo sapiens (human) / Production host: Homo sapiens (human) |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: HELICAL ARRAY / 3D reconstruction method: helical reconstruction |
-Sample preparation
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Source (natural) |
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Source (recombinant) |
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Buffer solution | pH: 7 | ||||||||||||||||||||||||||||||
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||||||||||||
Specimen support | Grid material: COPPER / Grid mesh size: 300 divisions/in. | ||||||||||||||||||||||||||||||
Vitrification | Cryogen name: ETHANE / Humidity: 95 % / Chamber temperature: 294 K |
-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: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
Electron lens | Mode: BRIGHT FIELDBright-field microscopy |
Image recording | Electron dose: 20 e/Å2 / Detector mode: INTEGRATING / Film or detector model: FEI FALCON II (4k x 4k) |
-Processing
EM software |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||||||||||
Helical symmerty | Angular rotation/subunit: -166.6 ° / Axial rise/subunit: 27.5 Å / Axial symmetry: C1 | ||||||||||||||||||||||||||||||||||||
3D reconstruction | Resolution: 11 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 5830 / Algorithm: BACK PROJECTION / Symmetry type: HELICAL | ||||||||||||||||||||||||||||||||||||
Atomic model building | Protocol: FLEXIBLE FIT / Space: REAL / Target criteria: Correlation coefficient |