|Entry||Database: EMDB / ID: 3743|
|Title||Straight filament in Alzheimer's disease brain|
|Function / homology||Caspase-mediated cleavage of cytoskeletal proteins / Tau and MAP proteins tubulin-binding repeat profile. / Tau and MAP proteins tubulin-binding repeat signature. / Tau and MAP protein, tubulin-binding repeat / Microtubule-associated protein Tau / Microtubule associated protein, tubulin-binding repeat / positive regulation of diacylglycerol kinase activity / plus-end-directed organelle transport along microtubule / neurofibrillary tangle assembly / axonal transport ...Caspase-mediated cleavage of cytoskeletal proteins / Tau and MAP proteins tubulin-binding repeat profile. / Tau and MAP proteins tubulin-binding repeat signature. / Tau and MAP protein, tubulin-binding repeat / Microtubule-associated protein Tau / Microtubule associated protein, tubulin-binding repeat / positive regulation of diacylglycerol kinase activity / plus-end-directed organelle transport along microtubule / neurofibrillary tangle assembly / axonal transport / histone-dependent DNA binding / negative regulation of establishment of protein localization to mitochondrion / neurofibrillary tangle / positive regulation of protein localization to synapse / phosphatidylinositol bisphosphate binding / regulation of chromosome organization / rRNA metabolic process / negative regulation of mitochondrial membrane potential / regulation of long term synaptic depression / tubulin complex / axon development / microtubule lateral binding / negative regulation of mitochondrial fission / microtubule polymerization / generation of neurons / lipoprotein particle binding / positive regulation of cellular protein localization / axonal transport of mitochondrion / negative regulation of tubulin deacetylation / intracellular distribution of mitochondria / AT DNA binding / regulation of mitochondrial fission / central nervous system neuron development / regulation of calcium-mediated signaling / somatodendritic compartment / negative regulation of kinase activity / cellular response to brain-derived neurotrophic factor stimulus / internal protein amino acid acetylation / regulation of microtubule polymerization / receptor ligand activity / dynactin binding / regulation of microtubule polymerization or depolymerization / supramolecular fiber organization / axolemma / stress granule assembly / cytoplasmic microtubule organization / main axon / regulation of response to DNA damage stimulus / synapse assembly / microtubule associated complex / positive regulation of axon extension / phosphatidylinositol binding / axon cytoplasm / protein phosphatase 2A binding / apolipoprotein binding / regulation of microtubule cytoskeleton organization / microglial cell activation / positive regulation of microtubule polymerization / nuclear periphery / synapse organization / amyloid fibril formation / regulation of autophagy / microtubule cytoskeleton organization / astrocyte activation / cellular response to nerve growth factor stimulus / cytoplasmic ribonucleoprotein granule / regulation of synaptic plasticity / Hsp90 protein binding / memory / positive regulation of superoxide anion generation / response to lead ion / protein binding, bridging / microtubule cytoskeleton / cellular response to reactive oxygen species / cell body / cellular response to heat / regulation of cellular response to heat / neuron projection development / single-stranded DNA binding / activation of cysteine-type endopeptidase activity involved in apoptotic process / growth cone / SH3 domain binding / positive regulation of neuron death / learning or memory / double-stranded DNA binding / actin binding / chaperone binding / cell-cell signaling / protein complex oligomerization / microtubule / protein homooligomerization / microtubule binding / dendritic spine / negative regulation of gene expression / sequence-specific DNA binding / nuclear speck / axon / neuronal cell body / dendrite / intracellular|
Function and homology information
|Source||Homo sapiens (human)|
|Method||helical reconstruction / cryo EM / 3.4 Å resolution|
|Authors||Fitzpatrick AWP / Falcon B / He S|
|Citation||Journal: Nature / Year: 2017|
Title: Cryo-EM structures of tau filaments from Alzheimer's disease.
Authors: Anthony W P Fitzpatrick / Benjamin Falcon / Shaoda He / Alexey G Murzin / Garib Murshudov / Holly J Garringer / R Anthony Crowther / Bernardino Ghetti / Michel Goedert / Sjors H W Scheres
|Validation Report||PDB-ID: 5o3t|
SummaryFull reportAbout validation report
|Date||Deposition: May 24, 2017 / Header (metadata) release: Jul 26, 2017 / Map release: Jul 26, 2017 / Last update: Aug 2, 2017|
|Structure viewer||EM map: |
Downloads & links
|File||emd_3743.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||Name: Tau / Number of components: 2|
-Component #2: protein, Microtubule-associated protein tau
|Protein||Name: Microtubule-associated protein tauTau protein / Recombinant expression: No|
|Mass||Theoretical: 7.940141 kDa|
|Source||Species: Homo sapiens (human)|
|Specimen||Specimen state: tissue / Method: cryo EM|
|Helical parameters||Axial symmetry: C1 (asymmetric) / Delta z: 4.74 Å / Delta phi: -1.05 deg.|
|Sample solution||Specimen conc.: 1 mg/ml|
Buffer solution: 20 mM Tris-HCl pH 7.4 containing 100 mM NaCl
|Vitrification||Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Temperature: 277.15 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: 900 - 3000 nm / Energy filter: GIF Quantum / Energy window: -10-10 eV|
|Specimen Holder||Model: FEI TITAN KRIOS AUTOGRID HOLDER|
|Camera||Detector: GATAN K2 QUANTUM (4k x 4k)|
|Image acquisition||Number of digital images: 1560|
Details: images were collected in movie-mode at 5 frames per second
|Processing||Method: helical reconstruction|
|3D reconstruction||Software: RELION / Resolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF|
-Atomic model buiding
|Modeling #1||Refinement protocol: flexible / Target criteria: Fourier shell correlation / Refinement space: RECIPROCAL|
Details: Fourier-space refinement of the complete atomic model against the paired helical filament and straight filament maps was performed in REFMAC. A stack of three consecutive monomers from each of the protofilaments was refined to preserve nearest-neighbour interactions for the middle chain.
Input PDB model: 2RNM
Chain ID: 2RNM_A
Overall bvalue: 114
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