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- EMDB-63785: Cryo-EM structure of dopaminated Tau fibril -

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Basic information

Entry
Database: EMDB / ID: EMD-63785
TitleCryo-EM structure of dopaminated Tau fibril
Map data
Sample
  • Organelle or cellular component: Cryo-EM structure of dopaminated Tau fibril
    • Protein or peptide: Microtubule-associated protein tau
KeywordsAmyloid / PROTEIN FIBRIL
Function / homology
Function and homology information


plus-end-directed organelle transport along microtubule / histone-dependent DNA binding / negative regulation of protein localization to mitochondrion / neurofibrillary tangle / microtubule lateral binding / axonal transport / tubulin complex / positive regulation of protein localization to synapse / phosphatidylinositol bisphosphate binding / generation of neurons ...plus-end-directed organelle transport along microtubule / histone-dependent DNA binding / negative regulation of protein localization to mitochondrion / neurofibrillary tangle / microtubule lateral binding / axonal transport / tubulin complex / positive regulation of protein localization to synapse / phosphatidylinositol bisphosphate binding / generation of neurons / rRNA metabolic process / axonal transport of mitochondrion / regulation of mitochondrial fission / axon development / regulation of chromosome organization / regulation of microtubule-based movement / central nervous system neuron development / intracellular distribution of mitochondria / minor groove of adenine-thymine-rich DNA binding / lipoprotein particle binding / microtubule polymerization / negative regulation of mitochondrial membrane potential / regulation of microtubule polymerization / dynactin binding / apolipoprotein binding / main axon / protein polymerization / axolemma / glial cell projection / Caspase-mediated cleavage of cytoskeletal proteins / regulation of microtubule polymerization or depolymerization / negative regulation of mitochondrial fission / neurofibrillary tangle assembly / positive regulation of axon extension / regulation of cellular response to heat / synapse assembly / Activation of AMPK downstream of NMDARs / regulation of long-term synaptic depression / positive regulation of superoxide anion generation / positive regulation of protein localization / cellular response to brain-derived neurotrophic factor stimulus / supramolecular fiber organization / cytoplasmic microtubule organization / regulation of calcium-mediated signaling / somatodendritic compartment / axon cytoplasm / positive regulation of microtubule polymerization / astrocyte activation / phosphatidylinositol binding / enzyme inhibitor activity / nuclear periphery / stress granule assembly / protein phosphatase 2A binding / regulation of microtubule cytoskeleton organization / cellular response to reactive oxygen species / Hsp90 protein binding / microglial cell activation / cellular response to nerve growth factor stimulus / synapse organization / PKR-mediated signaling / regulation of synaptic plasticity / protein homooligomerization / response to lead ion / SH3 domain binding / microtubule cytoskeleton organization / memory / regulation of autophagy / cytoplasmic ribonucleoprotein granule / neuron projection development / cell-cell signaling / single-stranded DNA binding / protein-folding chaperone binding / cellular response to heat / microtubule cytoskeleton / growth cone / actin binding / cell body / double-stranded DNA binding / protein-macromolecule adaptor activity / microtubule binding / sequence-specific DNA binding / dendritic spine / amyloid fibril formation / microtubule / learning or memory / neuron projection / membrane raft / axon / negative regulation of gene expression / neuronal cell body / DNA damage response / dendrite / protein kinase binding / enzyme binding / mitochondrion / DNA binding / RNA binding / extracellular region / identical protein binding / nucleus
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 speciesHomo sapiens (human)
Methodhelical reconstruction / cryo EM / Resolution: 3.55 Å
AuthorsLiu Z / Li X / Liu C
Funding support1 items
OrganizationGrant numberCountry
Not funded
CitationJournal: J Am Chem Soc / Year: 2026
Title: Dopamine-Induced Tau Modification Prevents Pathological Phosphorylation and Generates a Distinct Fibril Polymorph.
Authors: Zhengtao Liu / Xiang Li / Qianwen Wang / Kaien Liu / Wen Zeng / Danni Li / Kun Zhao / Yeyang Ma / Houfang Long / Shengnan Zhang / Dan Li / Bo Sun / Weidong Le / Chu Wang / Zhuohao He / ...Authors: Zhengtao Liu / Xiang Li / Qianwen Wang / Kaien Liu / Wen Zeng / Danni Li / Kun Zhao / Yeyang Ma / Houfang Long / Shengnan Zhang / Dan Li / Bo Sun / Weidong Le / Chu Wang / Zhuohao He / Wenyan Kang / Weidi Xiao / Cong Liu /
Abstract: Amyloid aggregation of tau is the key pathological event in various tauopathies including Alzheimer's and Pick's disease. Recently, dopamination was identified to modify tau on cysteine, which ...Amyloid aggregation of tau is the key pathological event in various tauopathies including Alzheimer's and Pick's disease. Recently, dopamination was identified to modify tau on cysteine, which protects against tau pathology, yet its structural and functional consequences remain unclear. Here, we show that dopamination of the three-repeat (3R) tau fragment K19 alleviates disease-associated tau phosphorylation and alters the tau fibril structure. Solution NMR analysis reveals that dopamine modification at Cys322 of tau suppresses phosphorylation at several pathogenic sites across the microtubule-binding region. Dopaminated tau also exhibited greatly diminished fibrillization and reduced seeding activity in cells. Finally, we determined the cryo-EM structure of dopaminated tau fibrils at 3.55 Å resolution, revealing a unique fibril polymorph with the smallest core region reported to date for tau. The dopaminated fibril core comprises only 11 residues (centered on the VQIVYK motif) and is stabilized by a minimal hydrophobic interface, explaining its decreased stability compared to that of unmodified tau fibrils. Our results provide atomic-level insight into how dopamine modification imparts a protective effect on tau and underscore the profound influence of post-translational modifications in modulating amyloid protein structure and pathology.
History
DepositionMar 17, 2025-
Header (metadata) releaseFeb 4, 2026-
Map releaseFeb 4, 2026-
UpdateFeb 4, 2026-
Current statusFeb 4, 2026Processing site: PDBc / Status: Released

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Structure visualization

Supplemental images

emd_63785.png

Downloads & links

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Map

FileDownload / File: emd_63785.map.gz / Format: CCP4 / Size: 91.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

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AxesZ (Sec.)Y (Row.)X (Col.)
1.06 Å/pix.
x 288 pix.
= 305.28 Å		1.06 Å/pix.
x 288 pix.
= 305.28 Å		1.06 Å/pix.
x 288 pix.
= 305.28 Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.06 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.0202
Minimum - Maximum-0.029311901 - 0.054119688
Average (Standard dev.)0.00012502831 (±0.001121053)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions288288288
Spacing288288288
CellA=B=C: 305.27997 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #1

Fileemd_63785_half_map_1.map
Projections & Slices
AxesZYX

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Slices (1/2)
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Histogram

Histogram (log scale)

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Half map: #2

Fileemd_63785_half_map_2.map
Projections & Slices
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Sample components

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Entire : Cryo-EM structure of dopaminated Tau fibril

EntireName: Cryo-EM structure of dopaminated Tau fibril
Components
  • Organelle or cellular component: Cryo-EM structure of dopaminated Tau fibril
    • Protein or peptide: Microtubule-associated protein tau

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Supramolecule #1: Cryo-EM structure of dopaminated Tau fibril

SupramoleculeName: Cryo-EM structure of dopaminated Tau fibril / type: organelle_or_cellular_component / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Microtubule-associated protein tau

MacromoleculeName: Microtubule-associated protein tau / type: protein_or_peptide / ID: 1 / Number of copies: 6 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 13.750876 KDa
Recombinant expressionOrganism: Escherichia coli K-12 (bacteria)
SequenceString:
QTAPVPMPDL KNVKSKIGST ENLKHQPGGG KVQIINKKLD LSNVQSKCGS KDNIKHVPGG GKVQIVYKPV DLSKVTSKCG SLGNIHHKP GGGQVEVKSE KLDFKDRVQS KIGSLDNITH VPGGGNKKIE

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: 6.5
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 55.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.4000000000000001 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Final reconstructionApplied symmetry - Helical parameters - Δz: 2.4007 Å
Applied symmetry - Helical parameters - Δ&Phi: 176.854 °
Applied symmetry - Helical parameters - Axial symmetry: C1 (asymmetric)
Resolution.type: BY AUTHOR / Resolution: 3.55 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 23890
CTF correctionType: NONE
Startup modelType of model: NONE
Final angle assignmentType: NOT APPLICABLE

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