+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-1909 | |||||||||
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Title | Skeletal thick filament showing myosin crowns and MyBP-C | |||||||||
Map data | Averaged thick filament tomogram showing myosin crowns and MyBP-C | |||||||||
Sample |
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Keywords | C-protein / myosin binding protein C / electron tomography / thick filament structure | |||||||||
Biological species | Anura (frogs and toads) | |||||||||
Method | subtomogram averaging / cryo EM / Resolution: 70.0 Å | |||||||||
Authors | Luther PK / Winkler H / Taylor K / Zoghbi ME / Craig R / Padron R / Squire JM / Liu J | |||||||||
Citation | Journal: Proc Natl Acad Sci U S A / Year: 2011 Title: Direct visualization of myosin-binding protein C bridging myosin and actin filaments in intact muscle. Authors: Pradeep K Luther / Hanspeter Winkler / Kenneth Taylor / Maria E Zoghbi / Roger Craig / Raúl Padrón / John M Squire / Jun Liu / Abstract: Myosin-binding protein C (MyBP-C) is a thick filament protein playing an essential role in muscle contraction, and MyBP-C mutations cause heart and skeletal muscle disease in millions worldwide. ...Myosin-binding protein C (MyBP-C) is a thick filament protein playing an essential role in muscle contraction, and MyBP-C mutations cause heart and skeletal muscle disease in millions worldwide. Despite its discovery 40 y ago, the mechanism of MyBP-C function remains unknown. In vitro studies suggest that MyBP-C could regulate contraction in a unique way--by bridging thick and thin filaments--but there has been no evidence for this in vivo. Here we use electron tomography of exceptionally well preserved muscle to demonstrate that MyBP-C does indeed bind to actin in intact muscle. This binding implies a physical mechanism for communicating the relative sliding between thick and thin filaments that does not involve myosin and which could modulate the contractile process. | |||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | EM map: SurfViewMolmilJmol/JSmol |
Supplemental images |
-Downloads & links
-EMDB archive
Map data | emd_1909.map.gz | 12.6 MB | EMDB map data format | |
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Header (meta data) | emd-1909-v30.xml emd-1909.xml | 7.5 KB 7.5 KB | Display Display | EMDB header |
Images | EMD-1909.png | 59 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-1909 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-1909 | HTTPS FTP |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_1909.map.gz / Format: CCP4 / Size: 13.4 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | Averaged thick filament tomogram showing myosin crowns and MyBP-C | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 11.5 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Sample components
-Entire : Thin section of fast-frozen/freeze substituted relaxed frog sarto...
Entire | Name: Thin section of fast-frozen/freeze substituted relaxed frog sartorius muscle. |
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Components |
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-Supramolecule #1000: Thin section of fast-frozen/freeze substituted relaxed frog sarto...
Supramolecule | Name: Thin section of fast-frozen/freeze substituted relaxed frog sartorius muscle. type: sample / ID: 1000 / Number unique components: 1 |
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Molecular weight | Experimental: 130 KDa / Theoretical: 130 KDa |
-Supramolecule #1: Thick filament
Supramolecule | Name: Thick filament / type: organelle_or_cellular_component / ID: 1 / Name.synonym: Thick filament / Recombinant expression: No / Database: NCBI |
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Source (natural) | Organism: Anura (frogs and toads) |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | subtomogram averaging |
-Sample preparation
Vitrification | Cryogen name: HELIUM / Instrument: OTHER |
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-Electron microscopy
Microscope | FEI/PHILIPS CM300FEG/T |
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Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy |
Sample stage | Specimen holder: Eucentric / Specimen holder model: OTHER |
-Image processing
Final reconstruction | Algorithm: OTHER / Resolution.type: BY AUTHOR / Resolution: 70.0 Å / Resolution method: OTHER / Software - Name: Protomo |
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-Atomic model buiding 1
Initial model | PDB ID: |
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Refinement | Space: REAL |