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- EMDB-62570: Cryo-EM structure of the TIA-1 prion-like domain amyloid fibril, WT -

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Basic information

Entry
Database: EMDB / ID: EMD-62570
TitleCryo-EM structure of the TIA-1 prion-like domain amyloid fibril, WT
Map data
Sample
  • Complex: Amyloid fibril formed by TIA-1 prion-like domain
    • Protein or peptide: Cytotoxic granule associated RNA binding protein TIA1
KeywordsAmyloid fibril / Prion-like domain / RNA-binding protein / PROTEIN FIBRIL
Function / homology
Function and homology information


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 ...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
TIA-1, RNA recognition motif 1 / TIA-1, RNA recognition motif 2 / TIAR, RNA recognition motif 3 / RNA recognition motif domain, eukaryote / RNA recognition motif / RNA recognition motif / RNA recognition motif / Eukaryotic RNA Recognition Motif (RRM) profile. / RNA recognition motif domain / RNA-binding domain superfamily / Nucleotide-binding alpha-beta plait domain superfamily
Similarity search - Domain/homology
Cytotoxic granule associated RNA binding protein TIA1
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodhelical reconstruction / cryo EM / Resolution: 3.36 Å
AuthorsInaoka 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
OrganizationGrant numberCountry
Ministry of Education, Culture, Sports, Science and Technology (Japan)JP22H05090 Japan
Japan Agency for Medical Research and Development (AMED)JP22ama121003 Japan
CitationJournal: To Be Published
Title: 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
DepositionDec 3, 2024-
Header (metadata) releaseDec 3, 2025-
Map releaseDec 3, 2025-
UpdateDec 3, 2025-
Current statusDec 3, 2025Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

Downloads & links

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Map

FileDownload / File: emd_62570.map.gz / Format: CCP4 / Size: 347.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
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Others
AxesZ (Sec.)Y (Row.)X (Col.)
1 Å/pix.
x 450 pix.
= 450. Å
1 Å/pix.
x 450 pix.
= 450. Å
1 Å/pix.
x 450 pix.
= 450. Å

Surface

Projections

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Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1 Å
Density
Contour LevelBy AUTHOR: 0.005
Minimum - Maximum-0.014952949 - 0.02774422
Average (Standard dev.)0.000011137963 (±0.00040079487)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions450450450
Spacing450450450
CellA=B=C: 450.0 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #1

Fileemd_62570_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Half map: #2

Fileemd_62570_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Sample components

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Entire : Amyloid fibril formed by TIA-1 prion-like domain

EntireName: Amyloid fibril formed by TIA-1 prion-like domain
Components
  • Complex: Amyloid fibril formed by TIA-1 prion-like domain
    • Protein or peptide: Cytotoxic granule associated RNA binding protein TIA1

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Supramolecule #1: Amyloid fibril formed by TIA-1 prion-like domain

SupramoleculeName: Amyloid fibril formed by TIA-1 prion-like domain / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Cytotoxic granule associated RNA binding protein TIA1

MacromoleculeName: Cytotoxic granule associated RNA binding protein TIA1 / type: protein_or_peptide / ID: 1 / Number of copies: 6 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 10.345128 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MGSSHHHHHH HHHHHHSENL YFQGGQYMPN GWQVPAYGMY GQAWNQQGFN QTQSSAPWMG PNYGVQPPQG QNGSMLPNQP SGYRVAGYE TQ

UniProtKB: Cytotoxic granule associated RNA binding protein TIA1

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Experimental details

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Structure determination

Methodcryo EM
Processinghelical reconstruction
Aggregation statefilament

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Sample preparation

BufferpH: 2 / Component - Concentration: 0.1 % / Component - Formula: CF3COOH / Component - Name: Trifluoroacetic acid
GridModel: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY
VitrificationCryogen name: ETHANE / Chamber humidity: 95 % / Chamber temperature: 277 K / Instrument: LEICA EM GP

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Electron microscopy

MicroscopeJEOL CRYO ARM 300
Specialist opticsEnergy filter - Name: In-column Omega Filter / Energy filter - Slit width: 20 eV
Image recordingFilm 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 beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination 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 stageSpecimen holder model: JEOL CRYOSPECPORTER / Cooling holder cryogen: NITROGEN

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Image processing

Final reconstructionApplied symmetry - Helical parameters - Δz: 2.38 Å
Applied symmetry - Helical parameters - Δ&Phi: 179.37 °
Applied symmetry - Helical parameters - Axial symmetry: C1 (asymmetric)
Resolution.type: BY AUTHOR / Resolution: 3.36 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 3.1) / Number images used: 56747
CTF correctionSoftware - Name: CTFFIND / Type: PHASE FLIPPING AND AMPLITUDE CORRECTION
Segment selectionNumber selected: 610417 / Software - Name: RELION (ver. 3.1)
Startup modelType of model: NONE
Final angle assignmentType: NOT APPLICABLE
FSC plot (resolution estimation)

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