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- PDB-10ij: S305I Frontotemporal Lobar Degeneration (FTLD) type I tau filament -

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Basic information

Entry
Database: PDB / ID: 10ij
TitleS305I Frontotemporal Lobar Degeneration (FTLD) type I tau filament
ComponentsMicrotubule-associated protein tau
KeywordsPROTEIN FIBRIL / tau / MAPT / FTD / FTLD / amyloid / neurodegeneration
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 / regulation of cellular response to heat / Activation of AMPK downstream of NMDARs / positive regulation of superoxide anion generation / positive regulation of protein localization / regulation of long-term synaptic depression / cellular response to brain-derived neurotrophic factor stimulus / supramolecular fiber organization / positive regulation of microtubule polymerization / cytoplasmic microtubule organization / somatodendritic compartment / synapse assembly / regulation of calcium-mediated signaling / axon cytoplasm / astrocyte activation / phosphatidylinositol binding / nuclear periphery / enzyme inhibitor activity / stress granule assembly / protein phosphatase 2A binding / regulation of microtubule cytoskeleton organization / regulation of autophagy / cellular response to reactive oxygen species / Hsp90 protein binding / microglial cell activation / cellular response to nerve growth factor stimulus / protein homooligomerization / synapse organization / PKR-mediated signaling / regulation of synaptic plasticity / response to lead ion / SH3 domain binding / microtubule cytoskeleton organization / memory / neuron projection development / cytoplasmic ribonucleoprotein granule / 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 / microtubule binding / sequence-specific DNA binding / protein-macromolecule adaptor activity / amyloid fibril formation / dendritic spine / microtubule / 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: 3.1 Å
AuthorsPan, H.S. / Merz, G.E. / Tse, E. / Southworth, D.R.
Funding support United States, 13items
OrganizationGrant numberCountry
Other privateA2023019F
National Institutes of Health/National Institute on Aging (NIH/NIA)P30AG062422 United States
National Institutes of Health/National Institute on Aging (NIH/NIA)P01AG019724 United States
National Institutes of Health/National Institute on Aging (NIH/NIA)U01AG057195 United States
National Institutes of Health/National Institute on Aging (NIH/NIA)U19AG063911 United States
Other private
Other private
National Institutes of Health/National Institute on Aging (NIH/NIA)U19: AG063911 United States
Other privateU54 NS092089
Other privateU01 AG045390
National Institutes of Health/National Institute on Aging (NIH/NIA)P01 AG019724 United States
National Institutes of Health/National Institute on Aging (NIH/NIA)P30 AG062422 United States
National Institutes of Health/National Institute on Aging (NIH/NIA)U24 AG21886) United States
CitationJournal: bioRxiv / Year: 2026
Title: Distinct tau filament folds in familial frontotemporal dementia due to the S305I mutation.
Authors: Henry S Pan / Gregory E Merz / Alissa Nana Li / Minh Quan Le / Hyunil Jo / Athena Quddus / Anthony Yung / Rian C Kormos / Arthur A Melo / Eliana Marisa Ramos / Argentina Lario Lago / ...Authors: Henry S Pan / Gregory E Merz / Alissa Nana Li / Minh Quan Le / Hyunil Jo / Athena Quddus / Anthony Yung / Rian C Kormos / Arthur A Melo / Eliana Marisa Ramos / Argentina Lario Lago / Salvatore Spina / Lea T Grinberg / Howard J Rosen / Eric Tse / Maria Luisa Gorno-Tempini / William F DeGrado / William W Seeley / Daniel R Southworth
Abstract: Frontotemporal lobar degeneration with tau inclusions (FTLD-tau) comprise a class of fatal heterogeneous neurodegenerative diseases. Approximately 10% arise from pathogenic MAPT mutations and often ...Frontotemporal lobar degeneration with tau inclusions (FTLD-tau) comprise a class of fatal heterogeneous neurodegenerative diseases. Approximately 10% arise from pathogenic MAPT mutations and often cause severe, early-onset disease with pathology that is distinct yet partially overlapping with sporadic cases. Here, we evaluated post-mortem tissue from a patient with FTLD-tau due to S305I showing neuropathology most consistent with argyrophilic grain disease (AGD), a prevalent limbic tauopathy of aging. Structures determined by cryo-electron microscopy reveal tau filament folds that differ from those found in sporadic AGD or other tauopathies and feature a 4-layer architecture stabilized by the Ile substitution within its core. Comparative structural analysis reveals conserved motifs are shared among AGD, corticobasal degeneration, and P301T. A well-defined density stacks along a cationic cleft, indicative of a bound RNA-like polyanion or small-molecule. analysis shows the S305I mutation promotes fibrilization relative to normal tau. These results demonstrate that stabilizes a distinct aggregation-prone tau fold that likely contributes to disease pathology and heterogeneity beyond its known splicing defects, and underscore potential limitations of using the most pathologically similar genetic form as a model for sporadic FTLD-tau.
History
DepositionJan 21, 2026Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 11, 2026Provider: repository / Type: Initial release
Revision 1.0Mar 11, 2026Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release
Revision 1.0Mar 11, 2026Data content type: FSC / Data content type: FSC / Provider: repository / Type: Initial release
Revision 1.0Mar 11, 2026Data content type: Half map / Part number: 1 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Mar 11, 2026Data content type: Half map / Part number: 2 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Mar 11, 2026Data content type: Image / Data content type: Image / Provider: repository / Type: Initial release
Revision 1.0Mar 11, 2026Data content type: Mask / Part number: 1 / Data content type: Mask / Provider: repository / Type: Initial release
Revision 1.0Mar 11, 2026Data content type: Primary map / Data content type: Primary map / Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Microtubule-associated protein tau
B: Microtubule-associated protein tau
C: Microtubule-associated protein tau
D: Microtubule-associated protein tau
E: Microtubule-associated protein tau
F: Microtubule-associated protein tau
G: Microtubule-associated protein tau
H: Microtubule-associated protein tau
I: Microtubule-associated protein tau
J: Microtubule-associated protein tau
K: Microtubule-associated protein tau


Theoretical massNumber of molelcules
Total (without water)127,18611
Polymers127,18611
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1

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Components

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


Mass: 11562.394 Da / Num. of mol.: 11 / Mutation: S305I
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human), (natural) Homo sapiens (human)
Production host: Escherichia coli (E. coli) / References: UniProt: P10636
Has protein modificationN

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Experimental details

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Experiment

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

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Sample preparation

ComponentName: Filaments purified S305I FTLD individual brain tissue / Type: TISSUE / Entity ID: all / Source: RECOMBINANT
Source (natural)Organism: Homo sapiens (human)
Buffer solutionpH: 7.4
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportGrid material: GOLD / Grid mesh size: 200 divisions/in. / Grid type: Quantifoil R1.2/1.3
VitrificationInstrument: FEI VITROBOT MARK IV / Cryogen 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 / Calibrated magnification: 105000 X / Nominal defocus max: 1800 nm / Nominal defocus min: 800 nm / C2 aperture diameter: 70 µm / Alignment procedure: COMA FREE
Specimen holderCryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER
Image recordingAverage exposure time: 5.4 sec. / Electron dose: 46 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) / Num. of grids imaged: 1 / Num. of real images: 7393

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Processing

EM software
IDNameVersionCategory
1RELION5.0.0particle selection
12RELION5.0.03D reconstruction
13PHENIX1.21.2model refinement
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Helical symmertyAngular rotation/subunit: 178.6 ° / Axial rise/subunit: 4.78 Å / Axial symmetry: C1
3D reconstructionResolution: 3.1 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 47171 / Symmetry type: HELICAL

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