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- EMDB-57273: AD fold in mouse injected with seeds of AD -

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Basic information

Entry
Database: EMDB / ID: EMD-57273
TitleAD fold in mouse injected with seeds of AD
Map dataSharpened map
Sample
  • Complex: Tau filament with the AD fold from mouse seeded by human AD tau seeds
    • Protein or peptide: Isoform Tau-A of Microtubule-associated protein tau
KeywordsAmyloid / prion / tau / Alzheimer's Disease. / STRUCTURAL PROTEIN
Function / homology
Function and homology information


negative regulation of tubulin deacetylation / Caspase-mediated cleavage of cytoskeletal proteins / negative regulation of intracellular transport / positive regulation of mesenchymal stem cell migration / positive regulation of long-term synaptic depression / PKR-mediated signaling / axon extension / mRNA transport / adult walking behavior / intrinsic apoptotic signaling pathway in response to oxidative stress ...negative regulation of tubulin deacetylation / Caspase-mediated cleavage of cytoskeletal proteins / negative regulation of intracellular transport / positive regulation of mesenchymal stem cell migration / positive regulation of long-term synaptic depression / PKR-mediated signaling / axon extension / mRNA transport / adult walking behavior / intrinsic apoptotic signaling pathway in response to oxidative stress / axo-dendritic transport / mitochondrion transport along microtubule / positive regulation of mitochondrial membrane potential / microtubule stabilizing activity / neurofibrillary tangle / microtubule lateral binding / tubulin complex / positive regulation of protein localization to synapse / regulation of microtubule-based movement / negative regulation of protein localization to mitochondrion / intracellular distribution of mitochondria / lipoprotein particle binding / negative regulation of mitochondrial membrane potential / microtubule polymerization / response to hyperoxia / apolipoprotein binding / regulation of calcium-mediated signaling / main axon / glial cell projection / regulation of microtubule polymerization or depolymerization / axoneme / axonal growth cone / negative regulation of mitochondrial fission / protein polymerization / positive regulation of axon extension / axolemma / regulation of cellular response to heat / positive regulation of microtubule polymerization / axonogenesis / heat shock protein binding / positive regulation of superoxide anion generation / positive regulation of protein localization / synapse assembly / somatodendritic compartment / supramolecular fiber organization / response to nutrient / nuclear periphery / protein phosphatase 2A binding / enzyme inhibitor activity / positive regulation of neuron projection development / SH3 domain binding / neuron migration / microtubule cytoskeleton organization / regulation of microtubule cytoskeleton organization / memory / Hsp90 protein binding / regulation of autophagy / protein homooligomerization / synapse organization / response to lead ion / neuron projection development / cytoplasmic ribonucleoprotein granule / microtubule cytoskeleton / microtubule / protein-folding chaperone binding / growth cone / cell body / microtubule binding / amyloid fibril formation / cytoplasmic side of plasma membrane / learning or memory / postsynaptic density / membrane raft / negative regulation of gene expression / axon / neuronal cell body / DNA damage response / dendrite / protein kinase binding / protein-containing complex binding / enzyme binding / DNA binding / extracellular region / identical protein binding / nucleus / plasma membrane / cytosol / cytoplasm
Similarity search - Function
Microtubule-associated protein Tau / Microtubule associated protein, tubulin-binding repeat / Tau and MAP protein, tubulin-binding repeat / Tau and MAP proteins tubulin-binding repeat signature. / Tau and MAP proteins tubulin-binding repeat profile. / :
Similarity search - Domain/homology
Microtubule-associated protein tau
Similarity search - Component
Biological speciesMus (mice) / Mus musculus (house mouse)
Methodhelical reconstruction / cryo EM / Resolution: 3.6 Å
AuthorsLovestam SL / Scheres SHW / Goedert M
Funding support United Kingdom, 1 items
OrganizationGrant numberCountry
Medical Research Council (MRC, United Kingdom) United Kingdom
CitationJournal: Nature / Year: 2026
Title: Prion-like transmission of human tau strains in the mouse brain.
Authors: Sofia Lövestam / Aki Shimozawa / Airi Tarutani / Reiko Ohtani / Masami Masuda-Suzukake / Kazuko Hasegawa / Andrew C Robinson / Yuko Saito / Shigeo Murayama / Mari Yoshida / Hisaomi Suzuki / ...Authors: Sofia Lövestam / Aki Shimozawa / Airi Tarutani / Reiko Ohtani / Masami Masuda-Suzukake / Kazuko Hasegawa / Andrew C Robinson / Yuko Saito / Shigeo Murayama / Mari Yoshida / Hisaomi Suzuki / Mitsumoto Onaya / Masato Hasegawa / Michel Goedert / Sjors H W Scheres /
Abstract: Most neurodegenerative diseases are thought to spread through the brain by prion-like mechanisms, in which filamentous protein assemblies self-propagate by templated seeding. Distinct conformations ...Most neurodegenerative diseases are thought to spread through the brain by prion-like mechanisms, in which filamentous protein assemblies self-propagate by templated seeding. Distinct conformations of amyloid filaments may provide the physical basis for the strains that lead to different diseases. However, a central pillar of the prion hypothesis, that strains retain their structural identity upon transmission, has not been demonstrated. Here we show that the injection of tau filaments from the brains of individuals with Alzheimer's disease or corticobasal degeneration into the brains of wild-type mice leads to the seeded assembly of amyloid filaments made of mouse tau with the same structures as those of the seeds. Thus, we show that, similar to prion strains, tau filaments propagate through templated seeding, and that the mouse is a suitable model to study the molecular mechanisms by which distinct tau folds drive disease-specific pathology in the brain.
History
DepositionMar 27, 2026-
Header (metadata) releaseMay 27, 2026-
Map releaseMay 27, 2026-
UpdateOct 14, 2026-
Current statusOct 14, 2026Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_57273.png

Downloads & links

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Map

FileDownload / File: emd_57273.map.gz / Format: CCP4 / Size: 27 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationSharpened map
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.49 Å/pix.
x 192 pix.
= 285.696 Å		1.49 Å/pix.
x 192 pix.
= 285.696 Å		1.49 Å/pix.
x 192 pix.
= 285.696 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.488 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.017
Minimum - Maximum-0.04054061 - 0.081556305
Average (Standard dev.)0.0008390014 (±0.0043275817)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions192192192
Spacing192192192
CellA=B=C: 285.696 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: Half map 1

Fileemd_57273_half_map_1.map
AnnotationHalf map 1
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Half map 2

Fileemd_57273_half_map_2.map
AnnotationHalf map 2
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Tau filament with the AD fold from mouse seeded by human AD tau seeds

EntireName: Tau filament with the AD fold from mouse seeded by human AD tau seeds
Components
  • Complex: Tau filament with the AD fold from mouse seeded by human AD tau seeds
    • Protein or peptide: Isoform Tau-A of Microtubule-associated protein tau

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Supramolecule #1: Tau filament with the AD fold from mouse seeded by human AD tau seeds

SupramoleculeName: Tau filament with the AD fold from mouse seeded by human AD tau seeds
type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Mus (mice)

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Macromolecule #1: Isoform Tau-A of Microtubule-associated protein tau

MacromoleculeName: Isoform Tau-A of Microtubule-associated protein tau / type: protein_or_peptide / ID: 1 / Number of copies: 6 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 44.961766 KDa
SequenceString: MADPRQEFDT MEDHAGDYTL LQDQEGDMDH GLKESPPQPP ADDGAEEPGS ETSDAKSTPT AEDVTAPLVD ERAPDKQAAA QPHTEIPEG ITAEEAGIGD TPNQEDQAAG HVTQARVASK DRTGNDEKKA KGADGKTGAK IATPRGAASP AQKGTSNATR I PAKTTPSP ...String:
MADPRQEFDT MEDHAGDYTL LQDQEGDMDH GLKESPPQPP ADDGAEEPGS ETSDAKSTPT AEDVTAPLVD ERAPDKQAAA QPHTEIPEG ITAEEAGIGD TPNQEDQAAG HVTQARVASK DRTGNDEKKA KGADGKTGAK IATPRGAASP AQKGTSNATR I PAKTTPSP KTPPGSGEPP KSGERSGYSS PGSPGTPGSR SRTPSLPTPP TREPKKVAVV RTPPKSPSAS KSRLQTAPVP MP DLKNVRS KIGSTENLKH QPGGGKVQII NKKLDLSNVQ SKCGSKDNIK HVPGGGSVQI VYKPVDLSKV TSKCGSLGNI HHK PGGGQV EVKSEKLDFK DRVQSKIGSL DNITHVPGGG NKKIETHKLT FRENAKAKTD HGAEIVYKSP VVSGDTSPRH LSNV SSTGS IDMVDSPQLA TLADEVSASL AKQGL

UniProtKB: Microtubule-associated protein tau

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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: 7.2
GridModel: Quantifoil / Material: GOLD / Mesh: 300
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 40.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.0 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Final reconstructionApplied symmetry - Helical parameters - Δz: 2.42 Å
Applied symmetry - Helical parameters - Δ&Phi: 179.446 °
Applied symmetry - Helical parameters - Axial symmetry: C1 (asymmetric)
Resolution.type: BY AUTHOR / Resolution: 3.6 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 5.1) / Number images used: 90623
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: OTHER / Details: De novo
Final angle assignmentType: NOT APPLICABLE
FSC plot (resolution estimation)

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