|Entry||Database: EMDB / ID: 0259|
|Title||Paired helical filament from sporadic Alzheimer's disease brain|
|Sample||Tau filaments extracted from the frontotemporal cortex of a patient with sporadic Alzheimer's disease|
|Function / homology||Microtubule associated protein, tubulin-binding repeat / Caspase-mediated cleavage of cytoskeletal proteins / Microtubule-associated protein Tau / Tau and MAP proteins tubulin-binding repeat signature. / Tau and MAP proteins tubulin-binding repeat profile. / Tau and MAP protein, tubulin-binding repeat / plus-end-directed organelle transport along microtubule / positive regulation of diacylglycerol kinase activity / neurofibrillary tangle assembly / axonal transport ...Microtubule associated protein, tubulin-binding repeat / Caspase-mediated cleavage of cytoskeletal proteins / Microtubule-associated protein Tau / Tau and MAP proteins tubulin-binding repeat signature. / Tau and MAP proteins tubulin-binding repeat profile. / Tau and MAP protein, tubulin-binding repeat / plus-end-directed organelle transport along microtubule / positive regulation of diacylglycerol kinase activity / neurofibrillary tangle assembly / axonal transport / histone-dependent DNA binding / negative regulation of establishment of protein localization to mitochondrion / regulation of chromosome organization / neurofibrillary tangle / positive regulation of protein localization to synapse / phosphatidylinositol bisphosphate binding / rRNA metabolic process / tubulin complex / microtubule lateral binding / generation of neurons / negative regulation of mitochondrial fission / lipoprotein particle binding / negative regulation of mitochondrial membrane potential / regulation of long-term synaptic depression / microtubule polymerization / axonal transport of mitochondrion / positive regulation of cellular protein localization / intracellular distribution of mitochondria / axon development / negative regulation of tubulin deacetylation / AT DNA binding / regulation of mitochondrial fission / central nervous system neuron development / regulation of calcium-mediated signaling / glial cell projection / negative regulation of kinase activity / internal protein amino acid acetylation / somatodendritic compartment / regulation of microtubule polymerization / dynactin binding / cellular response to brain-derived neurotrophic factor stimulus / receptor ligand activity / stress granule assembly / axolemma / supramolecular fiber organization / cytoplasmic microtubule organization / main axon / regulation of microtubule polymerization or depolymerization / regulation of response to DNA damage stimulus / positive regulation of axon extension / apolipoprotein binding / regulation of microtubule cytoskeleton organization / axon cytoplasm / positive regulation of microtubule polymerization / phosphatidylinositol binding / synapse assembly / nuclear periphery / amyloid fibril formation / synapse organization / microglial cell activation / regulation of autophagy / astrocyte activation / regulation of synaptic plasticity / cellular response to nerve growth factor stimulus / protein phosphatase 2A binding / cytoplasmic ribonucleoprotein granule / positive regulation of superoxide anion generation / microtubule cytoskeleton organization / memory / Hsp90 protein binding / cellular response to reactive oxygen species / protein binding, bridging / microtubule cytoskeleton / regulation of cellular response to heat / cell body / neuron projection development / single-stranded DNA binding / response to lead ion / activation of cysteine-type endopeptidase activity involved in apoptotic process / positive regulation of neuron death / SH3 domain binding / learning or memory / growth cone / double-stranded DNA binding / actin binding / cell-cell signaling / intracellular / cellular response to heat / chaperone binding / protein complex oligomerization / microtubule / microtubule binding / protein homooligomerization / dendritic spine / negative regulation of gene expression / sequence-specific DNA binding / nuclear speck / neuron projection / membrane raft / axon|
Function and homology information
|Method||helical reconstruction / cryo EM / 3.2 Å resolution|
|Authors||Falcon B / Zhang W / Schweighauser M / Murzin AG / Vidal R / Garringer HJ / Ghetti B / Scheres SHW / Goedert M|
|Citation||Journal: Acta Neuropathol. / Year: 2018|
Title: Tau filaments from multiple cases of sporadic and inherited Alzheimer's disease adopt a common fold.
Authors: Benjamin Falcon / Wenjuan Zhang / Manuel Schweighauser / Alexey G Murzin / Ruben Vidal / Holly J Garringer / Bernardino Ghetti / Sjors H W Scheres / Michel Goedert
|Validation Report||PDB-ID: 6hre|
SummaryFull reportAbout validation report
|Date||Deposition: Sep 26, 2018 / Header (metadata) release: Oct 10, 2018 / Map release: Oct 10, 2018 / Last update: Nov 7, 2018|
|Structure viewer||EM map: |
Downloads & links
|File||emd_0259.map.gz (map file in CCP4 format, 78733 KB)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 1.04 Å|
CCP4 map header:
-Entire Tau filaments extracted from the frontotemporal cortex of a patie...
|Entire||Name: Tau filaments extracted from the frontotemporal cortex of a patient with sporadic Alzheimer's disease|
Number of components: 2
-Component #1: cellular-component, Tau filaments extracted from the frontotempor...
|Cellular-component||Name: Tau filaments extracted from the frontotemporal cortex of a patient with sporadic Alzheimer's disease|
Recombinant expression: No
-Component #2: protein, Microtubule-associated protein tau
|Protein||Name: Microtubule-associated protein tauTau protein / Number of Copies: 6 / Recombinant expression: No|
|Mass||Theoretical: 45.919871 kDa|
|Source||Species: Human (human)|
|Source (natural)||Organ or tissue: Brain|
|Specimen||Specimen state: tissue / Method: cryo EM|
|Helical parameters||Axial symmetry: C1 (asymmetric) / Delta z: 2.37 Å / Delta phi: 179.45 deg.|
|Sample solution||Specimen conc.: 0.5 mg/ml / pH: 7.4|
|Vitrification||Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Temperature: 277 K / Humidity: 100 %|
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Imaging||Microscope: FEI TITAN KRIOS|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Electron dose: 1.2 e/Å2 / Illumination mode: FLOOD BEAM|
|Lens||Cs: 2.7 mm / Imaging mode: BRIGHT FIELD / Defocus: 1700.0 - 2800.0 nm / Energy filter: GIF Quantum LS|
|Specimen Holder||Model: OTHER|
|Camera||Detector: GATAN K2 QUANTUM (4k x 4k)|
|Processing||Method: helical reconstruction|
|3D reconstruction||Software: RELION / Resolution: 3.2 Å / Resolution method: FSC 0.143 CUT-OFF|
-Atomic model buiding
|Modeling #1||Target criteria: Fourier shell correlation / Refinement space: RECIPROCAL|
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.
Overall bvalue: 72.799999999999997
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