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Yorodumi- PDB-6cxi: Cardiac thin filament decorated with C0C1 fragment of cardiac myo... -
+Open data
-Basic information
Entry | Database: PDB / ID: 6cxi | ||||||
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Title | Cardiac thin filament decorated with C0C1 fragment of cardiac myosin binding protein C mode 1 | ||||||
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 / regulation of transepithelial transport / morphogenesis of a polarized epithelium / cardiac myofibril / regulation of striated muscle contraction / structural constituent of postsynaptic actin cytoskeleton ...basal body patch / C zone / regulation of muscle filament sliding / striated muscle myosin thick filament / tight junction assembly / regulation of transepithelial transport / morphogenesis of a polarized epithelium / cardiac myofibril / regulation of striated muscle contraction / structural constituent of postsynaptic actin cytoskeleton / profilin binding / protein localization to bicellular tight junction / dense body / Formation of annular gap junctions / Gap junction degradation / Cell-extracellular matrix interactions / Adherens junctions interactions / regulation of stress fiber assembly / positive regulation of ATP-dependent activity / Striated Muscle Contraction / Sensory processing of sound by outer hair cells of the cochlea / Interaction between L1 and Ankyrins / Sensory processing of sound by inner hair cells of the cochlea / regulation of synaptic vesicle endocytosis / A band / ventricular cardiac muscle tissue morphogenesis / structural constituent of muscle / apical junction complex / regulation of focal adhesion assembly / positive regulation of wound healing / myosin binding / maintenance of blood-brain barrier / myofibril / sarcomere organization / NuA4 histone acetyltransferase complex / myosin heavy chain binding / Recycling pathway of L1 / filamentous actin / calyx of Held / ATPase activator activity / EPH-ephrin mediated repulsion of cells / RHO GTPases Activate WASPs and WAVEs / RHO GTPases activate IQGAPs / RHOBTB2 GTPase cycle / heart morphogenesis / cardiac muscle contraction / titin binding / EPHB-mediated forward signaling / phagocytic vesicle / sarcomere / axonogenesis / Translocation of SLC2A4 (GLUT4) to the plasma membrane / RHO GTPases Activate Formins / cell motility / actin filament / 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 / Regulation of actin dynamics for phagocytic cup formation / platelet aggregation / VEGFA-VEGFR2 Pathway / cellular response to type II interferon / 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 / Signaling by BRAF and RAF1 fusions / cell-cell junction / Clathrin-mediated endocytosis / actin binding / angiogenesis / cytoskeleton / blood microparticle / hydrolase activity / cell adhesion / positive regulation of cell migration / axon / focal adhesion / ubiquitin protein ligase binding / synapse / positive regulation of gene expression / protein kinase binding / extracellular space / extracellular exosome / ATP binding / identical protein binding / membrane / nucleus / metal ion binding / plasma membrane / cytoplasm / cytosol 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 | 6cxi.cif.gz | 533.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6cxi.ent.gz | 428.4 KB | Display | PDB format |
PDBx/mmJSON format | 6cxi.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 6cxi_validation.pdf.gz | 1011.9 KB | Display | wwPDB validaton report |
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Full document | 6cxi_full_validation.pdf.gz | 1.1 MB | Display | |
Data in XML | 6cxi_validation.xml.gz | 82.5 KB | Display | |
Data in CIF | 6cxi_validation.cif.gz | 131.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cx/6cxi ftp://data.pdbj.org/pub/pdb/validation_reports/cx/6cxi | HTTPS FTP |
-Related structure data
Related structure data | 7780MC 4346C 7781C 6cxjC 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 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
Component |
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Molecular weight | Experimental value: NO | |||||||||||||||||||||||||||||||||||
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 | Instrument: FEI VITROBOT MARK II / 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 FIELD |
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: 6117 / Algorithm: BACK PROJECTION / Symmetry type: HELICAL | ||||||||||||||||||||||||||||||||||||
Atomic model building | Protocol: FLEXIBLE FIT / Space: REAL / Target criteria: Correlation coefficient |