[English] 日本語
![](img/lk-miru.gif)
- EMDB-4346: human cardiac myosin binding protein C C1 Ig-domain bound to nati... -
+
Open data
-
Basic information
Entry | Database: EMDB / ID: EMD-4346 | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | human cardiac myosin binding protein C C1 Ig-domain bound to native cardiac thin filament | |||||||||
![]() | ||||||||||
![]() |
| |||||||||
![]() | Cardiac thin filament regulator / CONTRACTILE PROTEIN | |||||||||
Function / homology | ![]() basal body patch / C zone / regulation of muscle filament sliding / striated muscle myosin thick filament / tight junction assembly / regulation of transepithelial transport / cardiac myofibril / morphogenesis of a polarized epithelium / regulation of striated muscle contraction / profilin binding ...basal body patch / C zone / regulation of muscle filament sliding / striated muscle myosin thick filament / tight junction assembly / regulation of transepithelial transport / cardiac myofibril / morphogenesis of a polarized epithelium / regulation of striated muscle contraction / profilin binding / protein localization to bicellular tight junction / structural constituent of postsynaptic actin cytoskeleton / dense body / Formation of annular gap junctions / Gap junction degradation / Cell-extracellular matrix interactions / regulation of stress fiber assembly / positive regulation of ATP-dependent activity / Adherens junctions interactions / 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 / A band / regulation of synaptic vesicle endocytosis / apical junction complex / structural constituent of muscle / ventricular cardiac muscle tissue morphogenesis / regulation of focal adhesion assembly / sarcomere organization / positive regulation of wound healing / myosin binding / myofibril / maintenance of blood-brain barrier / NuA4 histone acetyltransferase complex / myosin heavy chain binding / filamentous actin / Recycling pathway of L1 / 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 / phagocytic vesicle / EPHB-mediated forward signaling / sarcomere / axonogenesis / Translocation of SLC2A4 (GLUT4) to the plasma membrane / actin filament / cell motility / 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 / MAP2K and MAPK activation / Schaffer collateral - CA1 synapse / structural constituent of cytoskeleton / Regulation of actin dynamics for phagocytic cup formation / cellular response to type II interferon / 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 / Signaling by BRAF and RAF1 fusions / cell-cell junction / Clathrin-mediated endocytosis / actin binding / angiogenesis / blood microparticle / cytoskeleton / cell adhesion / hydrolase activity / 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 / cytosol / cytoplasm Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() | |||||||||
Method | helical reconstruction / cryo EM / Resolution: 9.0 Å | |||||||||
![]() | Risi C / Belknap B | |||||||||
Funding support | ![]()
| |||||||||
![]() | ![]() 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 |
|
-
Structure visualization
Movie |
![]() |
---|---|
Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
-
Downloads & links
-EMDB archive
Map data | ![]() | 1.4 MB | ![]() | |
---|---|---|---|---|
Header (meta data) | ![]() ![]() | 15.4 KB 15.4 KB | Display Display | ![]() |
Images | ![]() | 130.3 KB | ||
Filedesc metadata | ![]() | 6 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6g2tMC ![]() 7780C ![]() 7781C ![]() 6cxiC ![]() 6cxjC M: atomic model generated by this map C: citing same article ( |
---|---|
Similar structure data |
-
Links
EMDB pages | ![]() ![]() |
---|---|
Related items in Molecule of the Month |
-
Map
File | ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Voxel size | X=Y=Z: 2.1 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
|
-Supplemental data
-
Sample components
-Entire : human cardiac myosin binding protein C C1 Ig-domain bound to nati...
Entire | Name: human cardiac myosin binding protein C C1 Ig-domain bound to native cardiac thin filament |
---|---|
Components |
|
-Supramolecule #1: human cardiac myosin binding protein C C1 Ig-domain bound to nati...
Supramolecule | Name: human cardiac myosin binding protein C C1 Ig-domain bound to native cardiac thin filament type: complex / ID: 1 / Parent: 0 / Macromolecule list: all Details: Sample contains actin, tropomyosin, troponin complex, myosin binding protein-C C0-C1 Ig domains. Only C1 Ig-domain bound to the cardiac thin filament is visualized in the map |
---|
-Supramolecule #2: Actin, cytoplasmic 2
Supramolecule | Name: Actin, cytoplasmic 2 / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1 |
---|---|
Source (natural) | Organism: ![]() |
-Supramolecule #3: Myosin-binding protein C, cardiac-type
Supramolecule | Name: Myosin-binding protein C, cardiac-type / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #2 |
---|---|
Source (natural) | Organism: ![]() |
-Supramolecule #4: Tropomyosin
Supramolecule | Name: Tropomyosin / type: complex / ID: 4 / Parent: 1 / Macromolecule list: #3 |
---|---|
Source (natural) | Organism: ![]() ![]() |
-Macromolecule #1: Actin, cytoplasmic 2
Macromolecule | Name: Actin, cytoplasmic 2 / type: protein_or_peptide / ID: 1 / Number of copies: 6 / Enantiomer: LEVO |
---|---|
Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 41.838766 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MEEEIAALVI DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS KRGILTLKYP IEHGIVTNWD DMEKIWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM TQIMFETFNT PAMYVAIQAV LSLYASGRTT GIVMDSGDGV T HTVPIYEG ...String: MEEEIAALVI DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS KRGILTLKYP IEHGIVTNWD DMEKIWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM TQIMFETFNT PAMYVAIQAV LSLYASGRTT GIVMDSGDGV T HTVPIYEG YALPHAILRL DLAGRDLTDY LMKILTERGY SFTTTAEREI VRDIKEKLCY VALDFEQEMA TAASSSSLEK SY ELPDGQV ITIGNERFRC PEALFQPSFL GMESCGIHET TFNSIMKCDV DIRKDLYANT VLSGGTTMYP GIADRMQKEI TAL APSTMK IKIIAPPERK YSVWIGGSIL ASLSTFQQMW ISKQEYDESG PSIVHRKCF UniProtKB: Actin, cytoplasmic 2 |
-Macromolecule #2: Myosin-binding protein C, cardiac-type
Macromolecule | Name: Myosin-binding protein C, cardiac-type / type: protein_or_peptide / ID: 2 / Number of copies: 6 / Enantiomer: LEVO |
---|---|
Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 12.180806 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MDDPIGLFVM RPQDGEVTVG GSITFSARVA GASLLKPPVV KWFKGKWVDL SSKVGQHLQL HDSYDRASKV YLFELHITDA QPAFTGSYR CEVSTKDKFD CSNFNLTVHE UniProtKB: Myosin-binding protein C, cardiac-type |
-Macromolecule #3: Tropomyosin
Macromolecule | Name: Tropomyosin / type: protein_or_peptide / ID: 3 / Number of copies: 4 / Enantiomer: LEVO |
---|---|
Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 11.507176 KDa |
Sequence | String: (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) ...String: (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) |
-Experimental details
-Structure determination
Method | cryo EM |
---|---|
![]() | helical reconstruction |
Aggregation state | helical array |
-
Sample preparation
Buffer | pH: 7 |
---|---|
Grid | Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: LACEY / Pretreatment - Type: PLASMA CLEANING / Pretreatment - Time: 20 sec. / Pretreatment - Atmosphere: OTHER |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 95 % / Chamber temperature: 294 K / Instrument: FEI VITROBOT MARK II |
-
Electron microscopy
Microscope | FEI TITAN KRIOS |
---|---|
Image recording | Film or detector model: FEI FALCON II (4k x 4k) / Detector mode: INTEGRATING / Average electron dose: 20.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
-
Image processing
Final reconstruction | Applied symmetry - Helical parameters - Δz: 27.7 Å Applied symmetry - Helical parameters - Δ&Phi: -166.6 ° Applied symmetry - Helical parameters - Axial symmetry: C1 (asymmetric) Resolution.type: BY AUTHOR / Resolution: 9.0 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: SPIDER / Software - details: IHRSR / Number images used: 7051 |
---|---|
Startup model | Type of model: OTHER / Details: cylinder density map |
Final angle assignment | Type: NOT APPLICABLE / Software - Name: SPIDER / Software - details: IHRSR |
-Atomic model buiding 1
Refinement | Space: REAL / Protocol: FLEXIBLE FIT / Target criteria: Cross-correlation coefficient |
---|---|
Output model | ![]() PDB-6g2t: |