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- EMDB-51320: P301T type I tau filaments from human brain -

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Basic information

Entry
Database: EMDB / ID: EMD-51320
TitleP301T type I tau filaments from human brain
Map data
Sample
  • Tissue: P301T Type I Tau Protein Filament
    • Protein or peptide: Isoform Tau-D of Microtubule-associated protein tau
KeywordsP301T tau / Frontotemporal dementia and parkinsonism linked to chromosome 17 / Electron cryo-microscopy / PROTEIN FIBRIL
Function / homology
Function and homology information


plus-end-directed organelle transport along microtubule / histone-dependent DNA binding / neurofibrillary tangle assembly / : / negative regulation of establishment of protein localization to mitochondrion / neurofibrillary tangle / positive regulation of protein localization to synapse / microtubule lateral binding / axonal transport / main axon ...plus-end-directed organelle transport along microtubule / histone-dependent DNA binding / neurofibrillary tangle assembly / : / negative regulation of establishment of protein localization to mitochondrion / neurofibrillary tangle / positive regulation of protein localization to synapse / microtubule lateral binding / axonal transport / main axon / tubulin complex / regulation of long-term synaptic depression / phosphatidylinositol bisphosphate binding / negative regulation of tubulin deacetylation / negative regulation of kinase activity / generation of neurons / internal protein amino acid acetylation / regulation of chromosome organization / rRNA metabolic process / axonal transport of mitochondrion / regulation of mitochondrial fission / axon development / intracellular distribution of mitochondria / central nervous system neuron development / regulation of microtubule polymerization / microtubule polymerization / minor groove of adenine-thymine-rich DNA binding / lipoprotein particle binding / dynactin binding / negative regulation of mitochondrial membrane potential / glial cell projection / apolipoprotein binding / protein polymerization / negative regulation of mitochondrial fission / axolemma / regulation of microtubule polymerization or depolymerization / positive regulation of axon extension / Caspase-mediated cleavage of cytoskeletal proteins / regulation of microtubule cytoskeleton organization / synapse assembly / cytoplasmic microtubule organization / Activation of AMPK downstream of NMDARs / regulation of cellular response to heat / positive regulation of protein localization / supramolecular fiber organization / regulation of calcium-mediated signaling / axon cytoplasm / stress granule assembly / somatodendritic compartment / cellular response to brain-derived neurotrophic factor stimulus / positive regulation of microtubule polymerization / phosphatidylinositol binding / nuclear periphery / positive regulation of superoxide anion generation / protein phosphatase 2A binding / regulation of autophagy / astrocyte activation / cellular response to reactive oxygen species / response to lead ion / Hsp90 protein binding / microglial cell activation / synapse organization / cellular response to nerve growth factor stimulus / : / protein homooligomerization / regulation of synaptic plasticity / PKR-mediated signaling / memory / microtubule cytoskeleton organization / SH3 domain binding / cytoplasmic ribonucleoprotein granule / neuron projection development / microtubule cytoskeleton / cell-cell signaling / single-stranded DNA binding / actin binding / protein-folding chaperone binding / cellular response to heat / protein-macromolecule adaptor activity / cell body / growth cone / double-stranded DNA binding / microtubule binding / sequence-specific DNA binding / microtubule / dendritic spine / amyloid fibril formation / learning or memory / nuclear speck / neuron projection / membrane raft / axon / negative regulation of gene expression / neuronal cell body / dendrite / DNA damage response / protein kinase binding / enzyme binding / mitochondrion / DNA binding
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: 2.26 Å
AuthorsSchweighauser M / Shi Y / Murzin AG / Garringer HJ / Vidal R / Murrell JR / Erro ME / Seelaar H / Ferrer I / van Swieten JC ...Schweighauser M / Shi Y / Murzin AG / Garringer HJ / Vidal R / Murrell JR / Erro ME / Seelaar H / Ferrer I / van Swieten JC / Ghetti B / Scheres SHW / Goedert M
Funding support United Kingdom, China, United States, 6 items
OrganizationGrant numberCountry
Medical Research Council (MRC, United Kingdom)MC_UP_A025_1013 United Kingdom
Medical Research Council (MRC, United Kingdom)MC_1051284291 United Kingdom
National Natural Science Foundation of China (NSFC)82371415 China
National Institutes of Health/National Institute on Aging (NIH/NIA)P30-AG010133 United States
National Institutes of Health/National Institute on Aging (NIH/NIA)R01-AG080001 United States
National Institutes of Health/National Institute on Aging (NIH/NIA)RF1-AG071177 United States
CitationJournal: bioRxiv / Year: 2024
Title: Novel tau filament folds in individuals with mutations P301L and P301T.
Authors: Manuel Schweighauser / Yang Shi / Alexey G Murzin / Holly J Garringer / Ruben Vidal / Jill R Murrell / M Elena Erro / Harro Seelaar / Isidro Ferrer / John C van Swieten / Bernardino Ghetti / ...Authors: Manuel Schweighauser / Yang Shi / Alexey G Murzin / Holly J Garringer / Ruben Vidal / Jill R Murrell / M Elena Erro / Harro Seelaar / Isidro Ferrer / John C van Swieten / Bernardino Ghetti / Sjors H W Scheres / Michel Goedert /
Abstract: Mutations in , the microtubule-associated protein tau gene, give rise to cases of frontotemporal dementia and parkinsonism linked to chromosome 17 (FTDP-17) with abundant filamentous tau inclusions ...Mutations in , the microtubule-associated protein tau gene, give rise to cases of frontotemporal dementia and parkinsonism linked to chromosome 17 (FTDP-17) with abundant filamentous tau inclusions in brain cells. Individuals with pathological variants exhibit behavioural changes, cognitive impairment and signs of parkinsonism. Missense mutations of residue P301, which are the most common mutations associated with FTDP-17, give rise to the assembly of mutant four-repeat tau into filamentous inclusions, in the absence of extracellular deposits. Here we report the cryo-EM structures of tau filaments from five individuals belonging to three unrelated families with mutation P301L and from one individual belonging to a family with mutation P301T. A novel three-lobed tau fold resembling the two-layered tau fold of Pick's disease was present in all cases with the P301L tau mutation. Two different tau folds were found in the case with mutation P301T, the less abundant of which was a variant of the three-lobed fold. The major P301T tau fold was V-shaped, with partial similarity to the four-layered tau folds of corticobasal degeneration and argyrophilic grain disease. These findings suggest that FTDP-17 with mutations in P301 should be considered distinct inherited tauopathies and that model systems with these mutations should be used with caution in the study of sporadic tauopathies.
History
DepositionAug 12, 2024-
Header (metadata) releaseSep 11, 2024-
Map releaseSep 11, 2024-
UpdateSep 11, 2024-
Current statusSep 11, 2024Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_51320.png

Downloads & links

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Map

FileDownload / File: emd_51320.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
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AxesZ (Sec.)Y (Row.)X (Col.)
0.82 Å/pix.
x 400 pix.
= 329.6 Å		0.82 Å/pix.
x 400 pix.
= 329.6 Å		0.82 Å/pix.
x 400 pix.
= 329.6 Å

Surface

Projections

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Images are generated by Spider.

Voxel sizeX=Y=Z: 0.824 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.0125
Minimum - Maximum-0.021281838 - 0.054979462
Average (Standard dev.)0.00011700426 (±0.0019990068)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions400400400
Spacing400400400
CellA=B=C: 329.6 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_51320_msk_1.map
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Half map: #1

Fileemd_51320_half_map_1.map
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Half map: #2

Fileemd_51320_half_map_2.map
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Sample components

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Entire : P301T Type I Tau Protein Filament

EntireName: P301T Type I Tau Protein Filament
Components
  • Tissue: P301T Type I Tau Protein Filament
    • Protein or peptide: Isoform Tau-D of Microtubule-associated protein tau

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Supramolecule #1: P301T Type I Tau Protein Filament

SupramoleculeName: P301T Type I Tau Protein Filament / type: tissue / ID: 1 / Parent: 0 / Macromolecule list: all / Details: P301T tau filaments extracted from human brain.
Source (natural)Organism: Homo sapiens (human) / Organ: Brain / Tissue: Frontal Cortex

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

MacromoleculeName: Isoform Tau-D of Microtubule-associated protein tau / type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human) / Organ: Brain / Tissue: Frontal Cortex
Molecular weightTheoretical: 11.540303 KDa
SequenceString:
GKVQIINKKL DLSNVQSKCG SKDNIKHVTG GGSVQIVYKP VDLSKVTSKC GSLGNIHHKP GGGQVEVKSE KLDFKDRVQS KIGSLDNIT HVPGGGNKKI ETHKLTFR

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: 7.4
GridModel: Quantifoil R1.2/1.3 / Support film - Material: CARBON / Support film - topology: HOLEY
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 42.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.6 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: 4.76 Å
Applied symmetry - Helical parameters - Δ&Phi: -1.18 °
Applied symmetry - Helical parameters - Axial symmetry: C1 (asymmetric)
Resolution.type: BY AUTHOR / Resolution: 2.26 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 4.0) / Number images used: 102697
Startup modelType of model: NONE
Final angle assignmentType: NOT APPLICABLE
FSC plot (resolution estimation)

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Atomic model buiding 1

RefinementProtocol: AB INITIO MODEL
Output model

PDB-9gg1:
P301T type I tau filaments from human brain

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