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- PDB-10np: u-VT Ib tau filament from VT Case 1 -

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Basic information

Entry
Database: PDB / ID: 10np
Titleu-VT Ib tau filament from VT Case 1
ComponentsMicrotubule-associated protein tau
KeywordsSTRUCTURAL PROTEIN / Microtubule-associated protein
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 / axon development / axonal transport of mitochondrion / rRNA metabolic process / central nervous system neuron development / regulation of microtubule-based movement / regulation of mitochondrial fission / regulation of chromosome organization / 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 / regulation of calcium-mediated signaling / main axon / Caspase-mediated cleavage of cytoskeletal proteins / glial cell projection / regulation of microtubule polymerization or depolymerization / axolemma / positive regulation of axon extension / neurofibrillary tangle assembly / protein polymerization / negative regulation of mitochondrial fission / positive regulation of microtubule polymerization / regulation of cellular response to heat / positive regulation of superoxide anion generation / positive regulation of protein localization / Activation of AMPK downstream of NMDARs / cellular response to brain-derived neurotrophic factor stimulus / cytoplasmic microtubule organization / regulation of long-term synaptic depression / axon cytoplasm / supramolecular fiber organization / synapse assembly / somatodendritic compartment / astrocyte activation / nuclear periphery / phosphatidylinositol binding / protein phosphatase 2A binding / stress granule assembly / enzyme inhibitor activity / cellular response to reactive oxygen species / regulation of microtubule cytoskeleton organization / memory / microglial cell activation / cellular response to nerve growth factor stimulus / regulation of synaptic plasticity / Hsp90 protein binding / SH3 domain binding / synapse organization / regulation of autophagy / protein homooligomerization / microtubule cytoskeleton organization / PKR-mediated signaling / response to lead ion / neuron projection development / cytoplasmic ribonucleoprotein granule / microtubule cytoskeleton / cell-cell signaling / cellular response to heat / single-stranded DNA binding / growth cone / protein-folding chaperone binding / actin binding / cell body / double-stranded DNA binding / sequence-specific DNA binding / microtubule binding / amyloid fibril formation / dendritic spine / microtubule / learning or memory / protein-macromolecule adaptor activity / 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: 3.51 Å
AuthorsWatanabe, R. / Lee, E.B.
Funding support United States, 3items
OrganizationGrant numberCountry
National Institutes of Health/National Institute on Aging (NIH/NIA)RF1 AG065341 United States
National Institutes of Health/National Institute on Aging (NIH/NIA)P30 AG072979 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R35 GM142505 United States
CitationJournal: Nat.Struct.Mol.Biol. / Year: 2026
Title: Repositioning of polyubiquitin alters the pathologic tau filament structure
Authors: Watanabe, R. / Creekmore, B.C. / Darwich, N.F. / Smith, C.L. / Xu, H. / Baltazar, A. / Salphati, S. / Changolkar, L. / Hoxha, K. / Zhang, B. / O'Rourke, C.M. / Burslem, G.M. / Lee, V.M.-Y. / ...Authors: Watanabe, R. / Creekmore, B.C. / Darwich, N.F. / Smith, C.L. / Xu, H. / Baltazar, A. / Salphati, S. / Changolkar, L. / Hoxha, K. / Zhang, B. / O'Rourke, C.M. / Burslem, G.M. / Lee, V.M.-Y. / Chang, Y.-W. / Lee, E.B.
History
DepositionJan 28, 2026Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 2, 2026Provider: repository / Type: Initial release
Revision 1.0Sep 2, 2026Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
C: Microtubule-associated protein tau
E: Microtubule-associated protein tau
A: Microtubule-associated protein tau
D: Microtubule-associated protein tau
F: Microtubule-associated protein tau
B: Microtubule-associated protein tau
I: Microtubule-associated protein tau
K: Microtubule-associated protein tau
G: Microtubule-associated protein tau
J: Microtubule-associated protein tau
L: Microtubule-associated protein tau
H: Microtubule-associated protein tau
O: Microtubule-associated protein tau
Q: Microtubule-associated protein tau
M: Microtubule-associated protein tau
P: Microtubule-associated protein tau
R: Microtubule-associated protein tau
N: Microtubule-associated protein tau


Theoretical massNumber of molelcules
Total (without water)147,31918
Polymers147,31918
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

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


Mass: 8184.412 Da / Num. of mol.: 18 / Source method: isolated from a natural source / Source: (natural) 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: FILAMENT / 3D reconstruction method: helical reconstruction

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Sample preparation

ComponentName: tau filaments from VT / Type: COMPLEX / Entity ID: all / Source: NATURAL
Source (natural)Organism: Homo sapiens (human)
Buffer solutionpH: 7.4
SpecimenConc.: 0.91 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Details: Sarkosyl-insoluble proteins were extracted from the frontal neocortex of the patient's brain.
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: 2500 nm / Nominal defocus min: 500 nm
Image recordingElectron dose: 39.9 e/Å2 / Film or detector model: GATAN K3 (6k x 4k)
Image scansWidth: 5760 / Height: 4092

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Processing

EM software
IDNameCategory
1RELIONparticle selection
8PHENIXmodel refinement
13RELION3D reconstruction
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Helical symmertyAngular rotation/subunit: -1.21 ° / Axial rise/subunit: 4.78 Å / Axial symmetry: C1
3D reconstructionResolution: 3.51 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 39761 / Symmetry type: HELICAL
RefinementHighest resolution: 3.51 Å

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