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- PDB-29ou: CBD fold in mouse injected with seeds of CBD -

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Basic information

Entry
Database: PDB / ID: 29ou
TitleCBD fold in mouse injected with seeds of CBD
ComponentsIsoform Tau-A of Microtubule-associated protein tau
KeywordsSTRUCTURAL PROTEIN / Amyloid / prion / tau / Alzheimer's Disease.
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 / intrinsic apoptotic signaling pathway in response to oxidative stress / mitochondrion transport along microtubule ...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 / intrinsic apoptotic signaling pathway in response to oxidative stress / mitochondrion transport along microtubule / 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 / protein polymerization / main axon / regulation of microtubule polymerization or depolymerization / axoneme / negative regulation of mitochondrial fission / axolemma / glial cell projection / mRNA transport / axonal growth cone / positive regulation of axon extension / positive regulation of microtubule polymerization / regulation of cellular response to heat / positive regulation of protein localization / positive regulation of superoxide anion generation / supramolecular fiber organization / heat shock protein binding / regulation of calcium-mediated signaling / somatodendritic compartment / response to nutrient / synapse assembly / axonogenesis / nuclear periphery / enzyme inhibitor activity / protein phosphatase 2A binding / regulation of microtubule cytoskeleton organization / regulation of autophagy / Hsp90 protein binding / positive regulation of neuron projection development / protein homooligomerization / SH3 domain binding / synapse organization / response to lead ion / microtubule cytoskeleton organization / cytoplasmic side of plasma membrane / neuron migration / memory / neuron projection development / cytoplasmic ribonucleoprotein granule / growth cone / protein-folding chaperone binding / microtubule cytoskeleton / 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 (mice)
MethodELECTRON MICROSCOPY / helical reconstruction / cryo EM / Resolution: 3.4 Å
AuthorsLovestam, S.L. / Scheres, S.H.W. / Goedert, M.
Funding support United Kingdom, 1items
OrganizationGrant numberCountry
Medical Research Council (MRC, United Kingdom) United Kingdom
CitationJournal: To Be Published
Title: Prion-like transmission of human tau strains in the mouse brain
Authors: Lovestam, S. / Scheres, S.H.W. / Goeder, M. / Hasegawa, M.
History
DepositionMar 27, 2026Deposition site: PDBE / Processing site: PDBE
Revision 1.0May 27, 2026Provider: repository / Type: Initial release
Revision 1.0May 27, 2026Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release
Revision 1.0May 27, 2026Data content type: FSC / Data content type: FSC / Provider: repository / Type: Initial release
Revision 1.0May 27, 2026Data content type: Half map / Part number: 1 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0May 27, 2026Data content type: Half map / Part number: 2 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0May 27, 2026Data content type: Image / Data content type: Image / Provider: repository / Type: Initial release
Revision 1.0May 27, 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

Downloads & links

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Assembly

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


Theoretical massNumber of molelcules
Total (without water)134,8853
Polymers134,8853
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 Isoform Tau-A of Microtubule-associated protein tau / Neurofibrillary tangle protein / Paired helical filament-tau / PHF-tau


Mass: 44961.766 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) Mus (mice) / References: UniProt: P10637
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 filament with the CBD fold from mouse seeded by human CBD tau seeds
Type: COMPLEX / Entity ID: all / Source: NATURAL
Source (natural)Organism: Mus (mice)
Buffer solutionpH: 7.2
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: 2500 nm / Nominal defocus min: 1000 nm
Image recordingElectron dose: 40 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k)

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Processing

EM software
IDNameVersionCategory
1RELION5.1particle selection
13RELION5.13D reconstruction
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Helical symmertyAngular rotation/subunit: -0.89 ° / Axial rise/subunit: 4.87 Å / Axial symmetry: C1
3D reconstructionResolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 63967 / Symmetry type: HELICAL
Atomic model buildingPDB-ID: 6TJO

6tjo


Accession code: 6TJO / Source name: PDB / Type: experimental model

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