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- PDB-9shs: Head to Head tau filament with the Alzheimer's fold -

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Basic information

Entry
Database: PDB / ID: 9shs
TitleHead to Head tau filament with the Alzheimer's fold
ComponentsIsoform Tau-D of Microtubule-associated protein tau
KeywordsPROTEIN FIBRIL / TAU / HELICAL / FILAMENT / FIBRIL / AMYLOID / ALZHEIMER'S DISEASE / PAIRED HELICAL FILAMENT
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 microtubule-based movement / regulation of chromosome organization / intracellular distribution of mitochondria / central nervous system neuron development / 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 / Caspase-mediated cleavage of cytoskeletal proteins / regulation of microtubule polymerization or depolymerization / negative regulation of mitochondrial fission / glial cell projection / neurofibrillary tangle assembly / positive regulation of axon extension / positive regulation of microtubule polymerization / regulation of cellular response to heat / Activation of AMPK downstream of NMDARs / positive regulation of protein localization / positive regulation of superoxide anion generation / cellular response to brain-derived neurotrophic factor stimulus / supramolecular fiber organization / regulation of long-term synaptic depression / cytoplasmic microtubule organization / regulation of calcium-mediated signaling / somatodendritic compartment / axon cytoplasm / synapse assembly / astrocyte activation / phosphatidylinositol binding / nuclear periphery / enzyme inhibitor activity / protein phosphatase 2A binding / stress granule assembly / regulation of microtubule cytoskeleton organization / regulation of autophagy / cellular response to reactive oxygen species / microglial cell activation / cellular response to nerve growth factor stimulus / Hsp90 protein binding / protein homooligomerization / PKR-mediated signaling / SH3 domain binding / regulation of synaptic plasticity / synapse organization / response to lead ion / microtubule cytoskeleton organization / memory / cytoplasmic ribonucleoprotein granule / neuron projection development / cell-cell signaling / single-stranded DNA binding / cellular response to heat / growth cone / protein-folding chaperone binding / microtubule cytoskeleton / actin binding / cell body / double-stranded DNA binding / microtubule binding / sequence-specific DNA binding / amyloid fibril formation / dendritic spine / microtubule / protein-macromolecule adaptor activity / learning or memory / neuron projection / membrane raft / negative regulation of gene expression / axon / 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)
MethodELECTRON MICROSCOPY / helical reconstruction / cryo EM / Resolution: 3.4 Å
AuthorsScheres, S.H.W. / Goedert, M.
Funding support United Kingdom, 1items
OrganizationGrant numberCountry
Medical Research Council (MRC, United Kingdom) United Kingdom
CitationJournal: J Biol Chem / Year: 2025
Title: Seeding biosensor cell line that reproduces the Alzheimer tau fold.
Authors: Taxiarchis Katsinelos / Sofia Lövestam / Chao Qi / Benjamin Ryskeldi-Falcon / Jennifer A Macdonald / Gabriel Stephenson / Bernardino Ghetti / Ann McKee / Sjors H W Scheres / Michel Goedert /
Abstract: The assembly of tau protein into amyloid filaments through templated seeding is believed to underlie the propagation of pathology in neurodegenerative diseases, such as Alzheimer's disease (AD) and ...The assembly of tau protein into amyloid filaments through templated seeding is believed to underlie the propagation of pathology in neurodegenerative diseases, such as Alzheimer's disease (AD) and other tauopathies. A commonly used model system for studying this process is through the induction of tau filament formation in cultured cells following the addition of tau seeds isolated from the human brain. However, little is known about the structures of seeded filaments; some biosensor cell lines are unable to reproduce the tau filament structures from AD, because they overexpress tau fragments that do not cover the whole of the ordered filament core. Here, we describe a novel tau seeding biosensor model in human embryonic kidney 293T cells that overexpress residues K297-E391 of human 4R tau. The construct contains an N-terminal hemagglutinin tag, which allows the specific detection of the amplified template. The biosensor cells detected filaments seeded by material from sporadic three-repeat (3R) + four-repeat (4R) tauopathies, with little activity by seeds from 3R-only or 4R-only tauopathies. The sensitivity of seed detection from 3R + 4R tauopathies in our system was similar to or higher than for previously reported biosensors. We also structurally characterized the AD-seeded tau filaments by cryo-EM. Most of the cell-derived filaments consisted of two protofilaments with the Alzheimer's fold but with a "head-to-head" interprotofilament packing. Our results establish a sensitive biosensor cell line with specificity toward seeds from 3R + 4R tauopathies.
History
DepositionAug 27, 2025Deposition site: PDBE / Processing site: PDBE
Revision 1.0Oct 1, 2025Provider: repository / Type: Initial release
Revision 1.0Oct 1, 2025Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release
Revision 1.0Oct 1, 2025Data content type: FSC / Data content type: FSC / Provider: repository / Type: Initial release
Revision 1.0Oct 1, 2025Data content type: Half map / Part number: 1 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Oct 1, 2025Data content type: Half map / Part number: 2 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Oct 1, 2025Data content type: Image / Data content type: Image / Provider: repository / Type: Initial release
Revision 1.0Oct 1, 2025Data content type: Primary map / Data content type: Primary map / Provider: repository / Type: Initial release
Revision 1.1Dec 10, 2025Group: Data collection / Database references / Category: citation / citation_author / em_admin
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Revision 1.2Dec 24, 2025Group: Data collection / Database references / Category: citation / em_admin / Item: _citation.journal_volume / _em_admin.last_update
Revision 1.1Dec 24, 2025Data content type: EM metadata / Data content type: EM metadata / EM metadata / Group: Database references / Experimental summary / Data content type: EM metadata / EM metadata / Category: citation / em_admin / Data content type: EM metadata / EM metadata / Item: _citation.journal_volume / _em_admin.last_update

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Isoform Tau-D of Microtubule-associated protein tau
C: Isoform Tau-D of Microtubule-associated protein tau
E: Isoform Tau-D of Microtubule-associated protein tau
G: Isoform Tau-D of Microtubule-associated protein tau
B: Isoform Tau-D of Microtubule-associated protein tau
D: Isoform Tau-D of Microtubule-associated protein tau


Theoretical massNumber of molelcules
Total (without water)49,4496
Polymers49,4496
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area27860 Å2
ΔGint-60 kcal/mol
Surface area25200 Å2
MethodPISA

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Components

#1: Protein
Isoform Tau-D of Microtubule-associated protein tau / Neurofibrillary tangle protein / Paired helical filament-tau / PHF-tau


Mass: 8241.465 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: MAPT, MAPTL, MTBT1, TAU / Cell (production host): HEK293T / Production host: Homo sapiens (human) / References: UniProt: P10636
Has protein modificationN

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: HELICAL ARRAY / 3D reconstruction method: helical reconstruction

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Sample preparation

ComponentName: Tau filament / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT
Source (natural)Organism: Homo sapiens (human)
Source (recombinant)Organism: Homo sapiens (human) / Cell: HEK293T
Buffer solutionpH: 7.4
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: TFS KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 2800 nm / Nominal defocus min: 1700 nm / Cs: 2.7 mm
Image recordingElectron dose: 1.2 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k)

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Processing

EM software
IDNameVersionCategory
1RELIONparticle selection
13RELION53D reconstruction
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Helical symmertyAngular rotation/subunit: -0.93 ° / Axial rise/subunit: 4.83 Å / Axial symmetry: C2
3D reconstructionResolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 22000 / Symmetry type: HELICAL
Atomic model buildingB value: 72.8 / Protocol: AB INITIO MODEL / Space: RECIPROCAL / Target criteria: FOURIER SHELL CORRELATION
Details: FOURIER-SPACE REFINEMENT OF THE COMPLETE ATOMIC MODEL AGAINST THE NARROW PICK FILAMENT MAP WAS PERFORMED IN REFMAC. A STACK OF THREE CONSECUTIVE MONOMERS WAS REFINED TO PRESERVE NEAREST- ...Details: FOURIER-SPACE REFINEMENT OF THE COMPLETE ATOMIC MODEL AGAINST THE NARROW PICK FILAMENT MAP WAS PERFORMED IN REFMAC. A STACK OF THREE CONSECUTIVE MONOMERS WAS REFINED TO PRESERVE NEAREST-NEIGHBOUR INTERACTIONS FOR THE MIDDLE CHAIN.
RefinementHighest resolution: 3.4 Å

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