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Open data
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Basic information
| Entry | Database: EMDB / ID: EMD-0711 | |||||||||
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| Title | F-actin of cardiac thin filament in low-calcium state | |||||||||
Map data | F-actin in cardiac thin filament, low calcium state | |||||||||
Sample |
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Keywords | Cardiac thin filament / CONTRACTILE PROTEIN | |||||||||
| Function / homology | Function and homology informationFormation of the dystrophin-glycoprotein complex (DGC) / Striated Muscle Contraction / mesenchyme migration / striated muscle thin filament / skeletal muscle thin filament assembly / skeletal muscle fiber development / stress fiber / filopodium / actin filament / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement ...Formation of the dystrophin-glycoprotein complex (DGC) / Striated Muscle Contraction / mesenchyme migration / striated muscle thin filament / skeletal muscle thin filament assembly / skeletal muscle fiber development / stress fiber / filopodium / actin filament / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / lamellipodium / cell body / hydrolase activity / positive regulation of gene expression / protein-containing complex / ATP binding / cytoplasm Similarity search - Function | |||||||||
| Biological species | ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.0 Å | |||||||||
Authors | Oda T / Yanagisawa H | |||||||||
Citation | Journal: J Struct Biol / Year: 2020Title: Cryo-EM structures of cardiac thin filaments reveal the 3D architecture of troponin. Authors: Toshiyuki Oda / Haruaki Yanagisawa / Takeyuki Wakabayashi / ![]() Abstract: Troponin is an essential component of striated muscle and it regulates the sliding of actomyosin system in a calcium-dependent manner. Despite its importance, the structure of troponin has been ...Troponin is an essential component of striated muscle and it regulates the sliding of actomyosin system in a calcium-dependent manner. Despite its importance, the structure of troponin has been elusive due to its high structural heterogeneity. In this study, we analyzed the 3D structures of murine cardiac thin filaments using a cryo-electron microscope equipped with a Volta phase plate (VPP). Contrast enhancement by a VPP enabled us to reconstruct the entire repeat of the thin filament. We determined the orientation of troponin relative to F-actin and tropomyosin, and characterized the interactions between troponin and tropomyosin. This study provides a structural basis for understanding the molecular mechanism of actomyosin system. | |||||||||
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Structure visualization
| Movie |
Movie viewer |
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| Structure viewer | EM map: SurfView Molmil Jmol/JSmol |
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_0711.map.gz | 53.8 MB | EMDB map data format | |
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| Header (meta data) | emd-0711-v30.xml emd-0711.xml | 16.4 KB 16.4 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_0711_fsc.xml | 9.4 KB | Display | FSC data file |
| Images | emd_0711.png | 240.6 KB | ||
| Filedesc metadata | emd-0711.cif.gz | 6.1 KB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-0711 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-0711 | HTTPS FTP |
-Validation report
| Summary document | emd_0711_validation.pdf.gz | 189.8 KB | Display | EMDB validaton report |
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| Full document | emd_0711_full_validation.pdf.gz | 189.4 KB | Display | |
| Data in XML | emd_0711_validation.xml.gz | 502 B | Display | |
| Data in CIF | emd_0711_validation.cif.gz | 447 B | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-0711 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-0711 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 6kllMC ![]() 0712C ![]() 0714C ![]() 0715C ![]() 0717C ![]() 0718C ![]() 0796C ![]() 0797C ![]() 0798C ![]() 0799C ![]() 0802C ![]() 0804C ![]() 0805C ![]() 0806C ![]() 0807C ![]() 0808C ![]() 6klnC ![]() 6klpC ![]() 6klqC ![]() 6kltC ![]() 6kluC M: atomic model generated by this map C: citing same article ( |
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| Similar structure data | |
| EM raw data | EMPIAR-10348 (Title: Cardiac thin filament in low calcium state / Data size: 2.5 TBData #1: Unaligned multiframe micrographs of cardiac myofilaments in low calcium state [micrographs - multiframe]) |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_0711.map.gz / Format: CCP4 / Size: 70.2 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Annotation | F-actin in cardiac thin filament, low calcium state | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.07 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
CCP4 map header:
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-Supplemental data
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Sample components
-Entire : Cardiac thin filament
| Entire | Name: Cardiac thin filament |
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| Components |
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-Supramolecule #1: Cardiac thin filament
| Supramolecule | Name: Cardiac thin filament / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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| Source (natural) | Organism: ![]() |
-Macromolecule #1: Actin, alpha skeletal muscle
| Macromolecule | Name: Actin, alpha skeletal muscle / type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 41.875633 KDa |
| Sequence | String: DEDETTALVC DNGSGLVKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS KRGILTLKYP IE(HIC)GII TNW DDMEKIWHHT FYNELRVAPE EHPTLLTEAP LNPKANREKM TQIMFETFNV PAMYVAIQAV LSLYASGRTT GIVLDSG DG VTHNVPIYEG ...String: DEDETTALVC DNGSGLVKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS KRGILTLKYP IE(HIC)GII TNW DDMEKIWHHT FYNELRVAPE EHPTLLTEAP LNPKANREKM TQIMFETFNV PAMYVAIQAV LSLYASGRTT GIVLDSG DG VTHNVPIYEG YALPHAIMRL DLAGRDLTDY LMKILTERGY SFVTTAEREI VRDIKEKLCY VALDFENEMA TAASSSSL E KSYELPDGQV ITIGNERFRC PETLFQPSFI GMESAGIHET TYNSIMKCDI DIRKDLYANN VMSGGTTMYP GIADRMQKE ITALAPSTMK IKIIAPPERK YSVWIGGSIL ASLSTFQQMW ITKQEYDEAG PSIVHRKCF UniProtKB: Actin, alpha skeletal muscle |
-Macromolecule #2: MAGNESIUM ION
| Macromolecule | Name: MAGNESIUM ION / type: ligand / ID: 2 / Number of copies: 4 / Formula: MG |
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| Molecular weight | Theoretical: 24.305 Da |
-Macromolecule #3: ADENOSINE-5'-DIPHOSPHATE
| Macromolecule | Name: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 3 / Number of copies: 4 / Formula: ADP |
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| Molecular weight | Theoretical: 427.201 Da |
| Chemical component information | ![]() ChemComp-ADP: |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | filament |
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Sample preparation
| Concentration | 0.1 mg/mL |
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| Buffer | pH: 7.2 |
| Grid | Model: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 200 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 60 sec. / Pretreatment - Atmosphere: AIR |
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
| Microscope | FEI TITAN KRIOS |
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| Specialist optics | Phase plate: VOLTA PHASE PLATE / Energy filter - Name: GIF Bioquantum / Energy filter - Slit width: 20 eV |
| Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average exposure time: 5.6 sec. / Average electron dose: 60.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.1 µm / Nominal defocus min: 0.1 µm / Nominal magnification: 81000 |
| Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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