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- EMDB-18269: P301S Tau Filaments from the Brains of Tg2541 Transgenic Mouse Line -

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Basic information

Entry
Database: EMDB / ID: EMD-18269
TitleP301S Tau Filaments from the Brains of Tg2541 Transgenic Mouse Line
Map data
Sample
  • Tissue: P301S Tau Protein Filament (Tg2541)
    • Protein or peptide: Isoform Tau-E of Microtubule-associated protein tau
    • Protein or peptide: Unknown protein
    • Protein or peptide: Unknown protein
KeywordsP301S tau / Frontotemporal dementia and parkinsonism linked to chromosome 17 / Transgenic mice / Electron cryo-microscopy / PROTEIN FIBRIL
Function / homology
Function and homology information


Caspase-mediated cleavage of cytoskeletal proteins / negative regulation of intracellular transport / negative regulation of tubulin deacetylation / positive regulation of long-term synaptic depression / PKR-mediated signaling / axon extension / axo-dendritic transport / adult walking behavior / mitochondrion transport along microtubule / intrinsic apoptotic signaling pathway in response to oxidative stress ...Caspase-mediated cleavage of cytoskeletal proteins / negative regulation of intracellular transport / negative regulation of tubulin deacetylation / positive regulation of long-term synaptic depression / PKR-mediated signaling / axon extension / axo-dendritic transport / adult walking behavior / mitochondrion transport along microtubule / intrinsic apoptotic signaling pathway in response to oxidative stress / negative regulation of protein localization to mitochondrion / neurofibrillary tangle / microtubule lateral binding / tubulin complex / positive regulation of protein localization to synapse / regulation of microtubule-based movement / intracellular distribution of mitochondria / lipoprotein particle binding / microtubule polymerization / negative regulation of mitochondrial membrane potential / apolipoprotein binding / main axon / protein polymerization / axolemma / axoneme / regulation of microtubule polymerization or depolymerization / negative regulation of mitochondrial fission / mRNA transport / glial cell projection / positive regulation of axon extension / axonal growth cone / regulation of cellular response to heat / positive regulation of superoxide anion generation / positive regulation of protein localization / supramolecular fiber organization / heat shock protein binding / positive regulation of microtubule polymerization / synapse assembly / regulation of calcium-mediated signaling / somatodendritic compartment / response to nutrient / enzyme inhibitor activity / nuclear periphery / axonogenesis / protein phosphatase 2A binding / regulation of microtubule cytoskeleton organization / Hsp90 protein binding / positive regulation of neuron projection development / protein homooligomerization / synapse organization / regulation of autophagy / SH3 domain binding / response to lead ion / microtubule cytoskeleton organization / cytoplasmic side of plasma membrane / memory / neuron migration / neuron projection development / cytoplasmic ribonucleoprotein granule / protein-folding chaperone binding / microtubule cytoskeleton / growth cone / cell body / microtubule binding / amyloid fibril formation / microtubule / learning or memory / neuron projection / 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 / cytoplasm / cytosol
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 musculus (house mouse)
Methodhelical reconstruction / cryo EM / Resolution: 3.09 Å
AuthorsSchweighauser M / Murzin AG / Macdonald J / Lavenir I / Crowther RA / Scheres SHW / Goedert M
Funding support United Kingdom, 2 items
OrganizationGrant numberCountry
Medical Research Council (MRC, United Kingdom)MC-UP-A025-1013 United Kingdom
Medical Research Council (MRC, United Kingdom)MC-U105184291 United Kingdom
CitationJournal: Acta Neuropathol Commun / Year: 2023
Title: Cryo-EM structures of tau filaments from the brains of mice transgenic for human mutant P301S Tau.
Authors: Manuel Schweighauser / Alexey G Murzin / Jennifer Macdonald / Isabelle Lavenir / R Anthony Crowther / Sjors H W Scheres / Michel Goedert /
Abstract: Mice transgenic for human mutant P301S tau are widely used as models for human tauopathies. They develop neurodegeneration and abundant filamentous inclusions made of human mutant four-repeat tau. ...Mice transgenic for human mutant P301S tau are widely used as models for human tauopathies. They develop neurodegeneration and abundant filamentous inclusions made of human mutant four-repeat tau. Here we used electron cryo-microscopy (cryo-EM) to determine the structures of tau filaments from the brains of Tg2541 and PS19 mice. Both lines express human P301S tau (0N4R for Tg2541 and 1N4R for PS19) on mixed genetic backgrounds and downstream of different promoters (murine Thy1 for Tg2541 and murine Prnp for PS19). The structures of tau filaments from Tg2541 and PS19 mice differ from each other and those of wild-type tau filaments from human brains. The structures of tau filaments from the brains of humans with mutations P301L, P301S or P301T in MAPT are not known. Filaments from the brains of Tg2541 and PS19 mice share a substructure at the junction of repeats 2 and 3, which comprises residues I297-V312 of tau and includes the P301S mutation. The filament core from the brainstem of Tg2541 mice consists of residues K274-H329 of tau and two disconnected protein densities. Two non-proteinaceous densities are also in evidence. The filament core from the cerebral cortex of line PS19 extends from residues G271-P364 of tau. One strong non-proteinaceous density is also present. Unlike the tau filaments from human brains, the sequences following repeat 4 are missing from the cores of tau filaments from the brains of Tg2541 and PS19 mice.
History
DepositionAug 19, 2023-
Header (metadata) releaseOct 11, 2023-
Map releaseOct 11, 2023-
UpdateOct 18, 2023-
Current statusOct 18, 2023Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_18269.png

Downloads & links

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Map

FileDownload / File: emd_18269.map.gz / Format: CCP4 / Size: 40.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

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AxesZ (Sec.)Y (Row.)X (Col.)
1.15 Å/pix.
x 220 pix.
= 253. Å		1.15 Å/pix.
x 220 pix.
= 253. Å		1.15 Å/pix.
x 220 pix.
= 253. Å

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.15 Å
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Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.025
Minimum - Maximum-0.046236455 - 0.12216287
Average (Standard dev.)0.0004340104 (±0.005403687)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions220220220
Spacing220220220
CellA=B=C: 253.0 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_18269_msk_1.map
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Half map: #1

Fileemd_18269_half_map_1.map
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Half map: #2

Fileemd_18269_half_map_2.map
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Sample components

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Entire : P301S Tau Protein Filament (Tg2541)

EntireName: P301S Tau Protein Filament (Tg2541)
Components
  • Tissue: P301S Tau Protein Filament (Tg2541)
    • Protein or peptide: Isoform Tau-E of Microtubule-associated protein tau
    • Protein or peptide: Unknown protein
    • Protein or peptide: Unknown protein

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Supramolecule #1: P301S Tau Protein Filament (Tg2541)

SupramoleculeName: P301S Tau Protein Filament (Tg2541) / type: tissue / ID: 1 / Parent: 0 / Macromolecule list: all
Details: Human P301S tau filaments extracted from the brains of transgenic mouse line Tg2541
Source (natural)Organism: Mus musculus (house mouse) / Strain: Tg2541 / Organ: Brain / Tissue: Brainstem

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

MacromoleculeName: Isoform Tau-E of Microtubule-associated protein tau / type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse) / Strain: Tg2541 / Organ: Brain / Tissue: Brainstem
Molecular weightTheoretical: 5.961934 KDa
SequenceString:
KVQIINKKLD LSNVQSKCGS KDNIKHVSGG GSVQIVYKPV DLSKVTSKCG SLGNIH

UniProtKB: Microtubule-associated protein tau

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Macromolecule #2: Unknown protein

MacromoleculeName: Unknown protein / type: protein_or_peptide / ID: 2 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse) / Strain: Tg2541 / Organ: Brain / Tissue: Brainstem
Molecular weightTheoretical: 1.039273 KDa
SequenceString:
(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)

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Macromolecule #3: Unknown protein

MacromoleculeName: Unknown protein / type: protein_or_peptide / ID: 3 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse) / Strain: Tg2541 / Organ: Brain / Tissue: Brainstem
Molecular weightTheoretical: 869.063 Da
SequenceString:
(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)

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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: 7.4
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: COUNTING / Average electron dose: 34.2 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.4 µm / Nominal defocus min: 1.8 µm / Nominal magnification: 105000
Sample stageCooling holder cryogen: NITROGEN
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Final reconstructionApplied symmetry - Helical parameters - Δz: 4.75 Å
Applied symmetry - Helical parameters - Δ&Phi: -0.83 °
Applied symmetry - Helical parameters - Axial symmetry: C1 (asymmetric)
Resolution.type: BY AUTHOR / Resolution: 3.09 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 4.1) / Number images used: 22760
Startup modelType of model: NONE
Final angle assignmentType: NOT APPLICABLE
FSC plot (resolution estimation)

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