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- EMDB-53247: Tau Paired Helical Filaments using PAD12 for seeding in primary m... -

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Basic information

Entry
Database: EMDB / ID: EMD-53247
TitleTau Paired Helical Filaments using PAD12 for seeding in primary mouse neurons
Map dataSharpened map
Sample
  • Complex: Amyloid tau filament
    • Protein or peptide: Microtubule associate protein tau
KeywordsAlzheimer's Disease / Tau / filament / amyloid / PROTEIN FIBRIL
Biological speciesHomo sapiens (human)
Methodhelical reconstruction / cryo EM / Resolution: 2.95 Å
AuthorsLovestam S / Scheres SHW
Funding support United Kingdom, 1 items
OrganizationGrant numberCountry
Medical Research Council (MRC, United Kingdom) United Kingdom
CitationJournal: Nat Commun / Year: 2025
Title: Seed structure and phosphorylation in the fuzzy coat impact tau seeding competency.
Authors: Alysa Kasen / Sofia Lövestam / Libby Breton / Lindsay Meyerdirk / Jacob Alec McPhail / Kristin Piche / Ariel Louwrier / Colt D Capan / Hyoungjoo Lee / Sjors H W Scheres / Michael X Henderson /
Abstract: Tau misfolding into β-sheet-rich filaments and subsequent recruitment of monomeric tau are central to Alzheimer's disease (AD) pathogenesis. While cryo-EM has resolved the conformation of the AD tau ...Tau misfolding into β-sheet-rich filaments and subsequent recruitment of monomeric tau are central to Alzheimer's disease (AD) pathogenesis. While cryo-EM has resolved the conformation of the AD tau core, the structural features conferring biological activity remain unclear. Here, we investigated how tau filament core structure and post-translational modifications influence seeding capacity in neurons and mice. Our findings show that although filament structure impacts seeding, the AD tau core alone is insufficient to fully replicate AD tau's biological activity. The unstructured fuzzy coat, particularly phosphorylation within this region, is essential for full seeding competence. Importantly, recombinant tau filaments bearing twelve phospho-mimetic residues (PAD12 tau) and adopting the AD fold recapitulate the seeding activity of native AD tau. These results demonstrate that tau filament pathogenicity arises from the combined contributions of both the ordered core structure and post-translational modifications within the fuzzy coat, providing critical insights into mechanisms underlying tau-driven neurodegeneration.
History
DepositionMar 25, 2025-
Header (metadata) releaseNov 5, 2025-
Map releaseNov 5, 2025-
UpdateNov 5, 2025-
Current statusNov 5, 2025Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_53247.png

Downloads & links

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Map

FileDownload / File: emd_53247.map.gz / Format: CCP4 / Size: 216 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.)
0.82 Å/pix.
x 384 pix.
= 316.416 Å		0.82 Å/pix.
x 384 pix.
= 316.416 Å		0.82 Å/pix.
x 384 pix.
= 316.416 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

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Images are generated by Spider.

Voxel sizeX=Y=Z: 0.824 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.00568
Minimum - Maximum-0.013762571 - 0.030292187
Average (Standard dev.)0.000100896235 (±0.0013887744)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions384384384
Spacing384384384
CellA=B=C: 316.41602 Å
α=β=γ: 90.0 °

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Supplemental data

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Additional map: Unsharpened map

Fileemd_53247_additional_1.map
AnnotationUnsharpened map
Projections & Slices
AxesZYX

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Half map: HalfMap1

Fileemd_53247_half_map_1.map
AnnotationHalfMap1
Projections & Slices
AxesZYX

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Histogram

Histogram (log scale)

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Half map: Halfmap2

Fileemd_53247_half_map_2.map
AnnotationHalfmap2
Projections & Slices
AxesZYX

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Sample components

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Entire : Amyloid tau filament

EntireName: Amyloid tau filament
Components
  • Complex: Amyloid tau filament
    • Protein or peptide: Microtubule associate protein tau

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Supramolecule #1: Amyloid tau filament

SupramoleculeName: Amyloid tau filament / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all / Details: Tau filament
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 37.1 kDa/nm

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Macromolecule #1: Microtubule associate protein tau

MacromoleculeName: Microtubule associate protein tau / type: protein_or_peptide / ID: 1 / Details: 0N3R tau with 12 phosphomimetics / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
SequenceString: MAEPRQEFEV MEDHAGTYGL GDRKDQGGYT MHQDQEGDTD AGLKEEAGIG DTPSLEDEAA GHVTQARMVS KSKDGTGSDD KKAKGADGKT KIATPRGAAP PGQKGQANAT RIPAKTPPAP KDPPSSGEPP KSGDRSGYSS PGDPGDPGSR SRDPDLPDPP TREPKKVAVV ...String:
MAEPRQEFEV MEDHAGTYGL GDRKDQGGYT MHQDQEGDTD AGLKEEAGIG DTPSLEDEAA GHVTQARMVS KSKDGTGSDD KKAKGADGKT KIATPRGAAP PGQKGQANAT RIPAKTPPAP KDPPSSGEPP KSGDRSGYSS PGDPGDPGSR SRDPDLPDPP TREPKKVAVV RDPPKDPSSA KSRLQTAPVP MPDLKNVKSK IGSTENLKHQ PGGGKVQIVY KPVDLSKVTS KCGSLGNIHH KPGGGQVEVK SEKLDFKDRV QSKIGSLDNI THVPGGGNKK IETHKLTFRE NAKAKTDHGA EIVYKDPVVD GDDDPRHLSN VSSTGSIDMV DSPQLATLAD EVSASLAKQG L

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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 / Details: 20 mM HEPES, 250 mM NaCitrate, 4 mM TCEP, pH 7.28
GridModel: Quantifoil R1.2/1.3 / Mesh: 400
VitrificationCryogen name: ETHANE / Chamber humidity: 100 %

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 30.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.0 µm / Nominal defocus min: 0.5 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Final reconstructionApplied symmetry - Helical parameters - Δz: 2.41 Å
Applied symmetry - Helical parameters - Δ&Phi: 179.47 °
Applied symmetry - Helical parameters - Axial symmetry: C1 (asymmetric)
Resolution.type: BY AUTHOR / Resolution: 2.95 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 5.0) / Software - details: Blue version / Number images used: 33722
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: NONE
Final angle assignmentType: NOT APPLICABLE
FSC plot (resolution estimation)

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