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Yorodumi- EMDB-62570: Cryo-EM structure of the TIA-1 prion-like domain amyloid fibril, WT -
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Open data
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Basic information
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| Title | Cryo-EM structure of the TIA-1 prion-like domain amyloid fibril, WT | |||||||||
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Keywords | Amyloid fibril / Prion-like domain / RNA-binding protein / PROTEIN FIBRIL | |||||||||
| Function / homology | Function and homology informationprotein localization to cytoplasmic stress granule / nuclear stress granule / poly(A) binding / mRNA 3'-UTR AU-rich region binding / regulation of mRNA splicing, via spliceosome / positive regulation of epithelial cell apoptotic process / FGFR2 alternative splicing / negative regulation of cytokine production / regulation of alternative mRNA splicing, via spliceosome / stress granule assembly ...protein localization to cytoplasmic stress granule / nuclear stress granule / poly(A) binding / mRNA 3'-UTR AU-rich region binding / regulation of mRNA splicing, via spliceosome / positive regulation of epithelial cell apoptotic process / FGFR2 alternative splicing / negative regulation of cytokine production / regulation of alternative mRNA splicing, via spliceosome / stress granule assembly / RNA splicing / mRNA 3'-UTR binding / mRNA processing / cytoplasmic stress granule / negative regulation of translation / ribonucleoprotein complex / apoptotic process / RNA binding / nucleoplasm / nucleus / cytosol / cytoplasm Similarity search - Function | |||||||||
| Biological species | Homo sapiens (human) | |||||||||
| Method | helical reconstruction / cryo EM / Resolution: 3.36 Å | |||||||||
Authors | Inaoka D / Miyata T / Makino F / Ohtani Y / Ekari M / Kobayashi R / Imamura K / Sakamoto E / Kodama ST / Yoshida N ...Inaoka D / Miyata T / Makino F / Ohtani Y / Ekari M / Kobayashi R / Imamura K / Sakamoto E / Kodama ST / Yoshida N / Kato T / Namba K / Tochio H / Sekiyama N | |||||||||
| Funding support | Japan, 2 items
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Citation | Journal: To Be PublishedTitle: TIA-1 PLD amyloid fibril formation is suppressed by the ALS-associated mutation Authors: Inaoka D / Miyata T / Makino F / Ohtani Y / Ekari M / Kobayashi R / Imamura K / Sakamoto E / Kodama ST / Yoshida N / Kato T / Namba K / Tochio H / Sekiyama N | |||||||||
| History |
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_62570.map.gz | 20.8 MB | EMDB map data format | |
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| Header (meta data) | emd-62570-v30.xml emd-62570.xml | 18.2 KB 18.2 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_62570_fsc.xml | 15.9 KB | Display | FSC data file |
| Images | emd_62570.png | 73.7 KB | ||
| Filedesc metadata | emd-62570.cif.gz | 5.8 KB | ||
| Others | emd_62570_half_map_1.map.gz emd_62570_half_map_2.map.gz | 277.8 MB 277.8 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-62570 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-62570 | HTTPS FTP |
-Validation report
| Summary document | emd_62570_validation.pdf.gz | 747.8 KB | Display | EMDB validaton report |
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| Full document | emd_62570_full_validation.pdf.gz | 747.4 KB | Display | |
| Data in XML | emd_62570_validation.xml.gz | 21.4 KB | Display | |
| Data in CIF | emd_62570_validation.cif.gz | 28.7 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-62570 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-62570 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9ktyMC ![]() 9ktzC M: atomic model generated by this map C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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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_62570.map.gz / Format: CCP4 / Size: 347.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: #1
| File | emd_62570_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #2
| File | emd_62570_half_map_2.map | ||||||||||||
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| Density Histograms |
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Sample components
-Entire : Amyloid fibril formed by TIA-1 prion-like domain
| Entire | Name: Amyloid fibril formed by TIA-1 prion-like domain |
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| Components |
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-Supramolecule #1: Amyloid fibril formed by TIA-1 prion-like domain
| Supramolecule | Name: Amyloid fibril formed by TIA-1 prion-like domain / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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| Source (natural) | Organism: Homo sapiens (human) |
-Macromolecule #1: Cytotoxic granule associated RNA binding protein TIA1
| Macromolecule | Name: Cytotoxic granule associated RNA binding protein TIA1 / type: protein_or_peptide / ID: 1 / Number of copies: 6 / Enantiomer: LEVO |
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| Source (natural) | Organism: Homo sapiens (human) |
| Molecular weight | Theoretical: 10.345128 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MGSSHHHHHH HHHHHHSENL YFQGGQYMPN GWQVPAYGMY GQAWNQQGFN QTQSSAPWMG PNYGVQPPQG QNGSMLPNQP SGYRVAGYE TQ UniProtKB: Cytotoxic granule associated RNA binding protein TIA1 |
-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: 2 / Component - Concentration: 0.1 % / Component - Formula: CF3COOH / Component - Name: Trifluoroacetic acid |
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| Grid | Model: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY |
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 95 % / Chamber temperature: 277 K / Instrument: LEICA EM GP |
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Electron microscopy
| Microscope | JEOL CRYO ARM 300 |
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| Specialist optics | Energy filter - Name: In-column Omega Filter / Energy filter - Slit width: 20 eV |
| Image recording | Film or detector model: GATAN K3 (6k x 4k) / Number real images: 4650 / Average exposure time: 5.353 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 / Cs: 2.7 mm / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.0 µm / Nominal magnification: 50000 |
| Sample stage | Specimen holder model: JEOL CRYOSPECPORTER / Cooling holder cryogen: NITROGEN |
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About Yorodumi



Keywords
Homo sapiens (human)
Authors
Japan, 2 items
Citation



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Processing
FIELD EMISSION GUN
