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Yorodumi- EMDB-13511: Cryo-EM structure of young JASP-stabilized F-actin (central 3er) -
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Open data
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Basic information
| Entry | Database: EMDB / ID: EMD-13511 | ||||||||||||||||||
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| Title | Cryo-EM structure of young JASP-stabilized F-actin (central 3er) | ||||||||||||||||||
Map data | Sharpened map of the central three F-actin molecules filtered to local resolution | ||||||||||||||||||
Sample |
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| Function / homology | Function and homology informationcytoskeletal motor activator activity / myosin heavy chain binding / tropomyosin binding / actin filament bundle / troponin I binding / filamentous actin / mesenchyme migration / actin filament bundle assembly / skeletal muscle myofibril / striated muscle thin filament ...cytoskeletal motor activator activity / myosin heavy chain binding / tropomyosin binding / actin filament bundle / troponin I binding / filamentous actin / mesenchyme migration / actin filament bundle assembly / skeletal muscle myofibril / striated muscle thin filament / skeletal muscle thin filament assembly / actin monomer binding / skeletal muscle fiber development / stress fiber / titin binding / actin filament polymerization / filopodium / actin filament / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / calcium-dependent protein binding / lamellipodium / cell body / hydrolase activity / protein domain specific binding / calcium ion binding / positive regulation of gene expression / magnesium ion binding / ATP binding / identical protein binding / cytoplasm Similarity search - Function | ||||||||||||||||||
| Biological species | ![]() ![]() | ||||||||||||||||||
| Method | helical reconstruction / cryo EM / Resolution: 3.1 Å | ||||||||||||||||||
Authors | Pospich S / Sweeney HL / Houdusse A / Raunser S | ||||||||||||||||||
| Funding support | Germany, European Union, France, United States, 5 items
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Citation | Journal: Elife / Year: 2021Title: High-resolution structures of the actomyosin-V complex in three nucleotide states provide insights into the force generation mechanism. Authors: Sabrina Pospich / H Lee Sweeney / Anne Houdusse / Stefan Raunser / ![]() Abstract: The molecular motor myosin undergoes a series of major structural transitions during its force-producing motor cycle. The underlying mechanism and its coupling to ATP hydrolysis and actin binding are ...The molecular motor myosin undergoes a series of major structural transitions during its force-producing motor cycle. The underlying mechanism and its coupling to ATP hydrolysis and actin binding are only partially understood, mostly due to sparse structural data on actin-bound states of myosin. Here, we report 26 high-resolution cryo-EM structures of the actomyosin-V complex in the strong-ADP, rigor, and a previously unseen post-rigor transition state that binds the ATP analog AppNHp. The structures reveal a high flexibility of myosin in each state and provide valuable insights into the structural transitions of myosin-V upon ADP release and binding of AppNHp, as well as the actomyosin interface. In addition, they show how myosin is able to specifically alter the structure of F-actin. | ||||||||||||||||||
| History |
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Structure visualization
| Movie |
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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_13511.map.gz | 957.2 KB | EMDB map data format | |
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| Header (meta data) | emd-13511-v30.xml emd-13511.xml | 23 KB 23 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_13511_fsc.xml | 11.7 KB | Display | FSC data file |
| Images | emd_13511.png | 96.6 KB | ||
| Masks | emd_13511_msk_1.map | 125 MB | Mask map | |
| Others | emd_13511_additional_1.map.gz emd_13511_additional_2.map.gz emd_13511_half_map_1.map.gz emd_13511_half_map_2.map.gz | 9.2 MB 1.2 MB 60.1 MB 60.1 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-13511 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-13511 | HTTPS FTP |
-Validation report
| Summary document | emd_13511_validation.pdf.gz | 420.9 KB | Display | EMDB validaton report |
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| Full document | emd_13511_full_validation.pdf.gz | 420.5 KB | Display | |
| Data in XML | emd_13511_validation.xml.gz | 18.1 KB | Display | |
| Data in CIF | emd_13511_validation.cif.gz | 23.6 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-13511 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-13511 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 7pm3MC ![]() 7pltC ![]() 7pluC ![]() 7plvC ![]() 7plwC ![]() 7plxC ![]() 7plyC ![]() 7plzC ![]() 7pm0C ![]() 7pm1C ![]() 7pm2C ![]() 7pm5C ![]() 7pm6C ![]() 7pm7C ![]() 7pm8C ![]() 7pm9C ![]() 7pmaC ![]() 7pmbC ![]() 7pmcC ![]() 7pmdC ![]() 7pmeC ![]() 7pmfC ![]() 7pmgC ![]() 7pmhC ![]() 7pmiC ![]() 7pmjC ![]() 7pmlC M: atomic model generated by this map C: citing same article ( |
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| Similar structure data |
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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_13511.map.gz / Format: CCP4 / Size: 125 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Annotation | Sharpened map of the central three F-actin molecules filtered to local resolution | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.1 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Mask #1
| File | emd_13511_msk_1.map | ||||||||||||
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| Density Histograms |
-Additional map: Denoised map of the central three F-actin molecules (LAFTER)
| File | emd_13511_additional_1.map | ||||||||||||
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| Annotation | Denoised map of the central three F-actin molecules (LAFTER) | ||||||||||||
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| Density Histograms |
-Additional map: Sharpened map of the central three F-actin molecules...
| File | emd_13511_additional_2.map | ||||||||||||
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| Annotation | Sharpened map of the central three F-actin molecules filtered to nominal resolution | ||||||||||||
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| Density Histograms |
-Half map: Half map of full filament
| File | emd_13511_half_map_1.map | ||||||||||||
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| Annotation | Half map of full filament | ||||||||||||
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| Density Histograms |
-Half map: Half map of full filament
| File | emd_13511_half_map_2.map | ||||||||||||
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| Annotation | Half map of full filament | ||||||||||||
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| Density Histograms |
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Sample components
-Entire : Young JASP-stabilized F-actin
| Entire | Name: Young JASP-stabilized F-actin |
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| Components |
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-Supramolecule #1: Young JASP-stabilized F-actin
| Supramolecule | Name: Young JASP-stabilized F-actin / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 Details: Young ADP-Pi-bound F-actin stabilized with jasplakinolide |
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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: 3 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 42.109973 KDa |
| Sequence | String: MCDEDETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA QSKRGILTLK YPIE(HIC)G IIT NWDDMEKIWH HTFYNELRVA PEEHPTLLTE APLNPKANRE KMTQIMFETF NVPAMYVAIQ AVLSLYASGR TTGIVLD SG DGVTHNVPIY ...String: MCDEDETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA QSKRGILTLK YPIE(HIC)G IIT NWDDMEKIWH HTFYNELRVA PEEHPTLLTE APLNPKANRE KMTQIMFETF NVPAMYVAIQ AVLSLYASGR TTGIVLD SG DGVTHNVPIY EGYALPHAIM RLDLAGRDLT DYLMKILTER GYSFVTTAER EIVRDIKEKL CYVALDFENE MATAASSS S LEKSYELPDG QVITIGNERF RCPETLFQPS FIGMESAGIH ETTYNSIMKC DIDIRKDLYA NNVMSGGTTM YPGIADRMQ KEITALAPST MKIKIIAPPE RKYSVWIGGS ILASLSTFQQ MWITKQEYDE AGPSIVHRKC F |
-Macromolecule #2: ADENOSINE-5'-DIPHOSPHATE
| Macromolecule | Name: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 2 / Number of copies: 3 / Formula: ADP |
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| Molecular weight | Theoretical: 427.201 Da |
| Chemical component information | ![]() ChemComp-ADP: |
-Macromolecule #3: PHOSPHATE ION
| Macromolecule | Name: PHOSPHATE ION / type: ligand / ID: 3 / Number of copies: 3 / Formula: PO4 |
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| Molecular weight | Theoretical: 94.971 Da |
| Chemical component information | ![]() ChemComp-PO4: |
-Macromolecule #4: MAGNESIUM ION
| Macromolecule | Name: MAGNESIUM ION / type: ligand / ID: 4 / Number of copies: 3 / Formula: MG |
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| Molecular weight | Theoretical: 24.305 Da |
-Macromolecule #5: Jasplakinolide
| Macromolecule | Name: Jasplakinolide / type: ligand / ID: 5 / Number of copies: 3 / Formula: 9UE |
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| Molecular weight | Theoretical: 709.67 Da |
| Chemical component information | ![]() ChemComp-9UE: |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | helical reconstruction |
| Aggregation state | filament |
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Sample preparation
| Buffer | pH: 7.5 |
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| Grid | Model: Quantifoil R2/1 / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE |
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 286 K / Instrument: FEI VITROBOT MARK III |
| Details | Rise 27.9 A, Twist -166.9 degrees |
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Electron microscopy
| Microscope | FEI TITAN KRIOS |
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| Specialist optics | Spherical aberration corrector: Cs-corrected microscope / Energy filter - Name: GIF Bioquantum / Energy filter - Slit width: 20 eV |
| Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: SUPER-RESOLUTION / Number grids imaged: 1 / Number real images: 1064 / Average exposure time: 15.0 sec. / Average electron dose: 80.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD / Cs: 0.0 mm |
| 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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About Yorodumi



Authors
Germany, European Union,
France,
United States, 5 items
Citation
UCSF Chimera

































































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