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Open data
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Basic information
Entry | Database: PDB / ID: 7p67 | |||||||||||||||||||||||||||||||||||||||
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Title | Globular glial tauopathy type 2 tau filament | |||||||||||||||||||||||||||||||||||||||
![]() | Microtubule-associated protein tau![]() | |||||||||||||||||||||||||||||||||||||||
![]() | PROTEIN FIBRIL / ![]() | |||||||||||||||||||||||||||||||||||||||
Function / homology | ![]() plus-end-directed organelle transport along microtubule / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | |||||||||||||||||||||||||||||||||||||||
Biological species | ![]() ![]() | |||||||||||||||||||||||||||||||||||||||
Method | ![]() ![]() | |||||||||||||||||||||||||||||||||||||||
![]() | Shi, Y. / Zhang, W. / Yang, Y. / Murzin, A.G. / Falcon, B. / Kotecha, A. / van Beers, M. / Tarutani, A. / Kametani, F. / Garringer, H.J. ...Shi, Y. / Zhang, W. / Yang, Y. / Murzin, A.G. / Falcon, B. / Kotecha, A. / van Beers, M. / Tarutani, A. / Kametani, F. / Garringer, H.J. / Vidal, R. / Hallinan, G.I. / Lashley, T. / Saito, Y. / Murayama, S. / Yoshida, M. / Tanaka, H. / Kakita, A. / Ikeuchi, T. / Robinson, A.C. / Mann, D.M.A. / Kovacs, G.G. / Revesz, T. / Ghetti, B. / Hasegawa, M. / Goedert, M. / Scheres, S.H.W. | |||||||||||||||||||||||||||||||||||||||
Funding support | ![]() ![]() ![]()
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![]() | ![]() Title: Structure-based classification of tauopathies. Authors: Yang Shi / Wenjuan Zhang / Yang Yang / Alexey G Murzin / Benjamin Falcon / Abhay Kotecha / Mike van Beers / Airi Tarutani / Fuyuki Kametani / Holly J Garringer / Ruben Vidal / Grace I ...Authors: Yang Shi / Wenjuan Zhang / Yang Yang / Alexey G Murzin / Benjamin Falcon / Abhay Kotecha / Mike van Beers / Airi Tarutani / Fuyuki Kametani / Holly J Garringer / Ruben Vidal / Grace I Hallinan / Tammaryn Lashley / Yuko Saito / Shigeo Murayama / Mari Yoshida / Hidetomo Tanaka / Akiyoshi Kakita / Takeshi Ikeuchi / Andrew C Robinson / David M A Mann / Gabor G Kovacs / Tamas Revesz / Bernardino Ghetti / Masato Hasegawa / Michel Goedert / Sjors H W Scheres / ![]() ![]() ![]() ![]() ![]() ![]() Abstract: The ordered assembly of tau protein into filaments characterizes several neurodegenerative diseases, which are called tauopathies. It was previously reported that, by cryo-electron microscopy, the ...The ordered assembly of tau protein into filaments characterizes several neurodegenerative diseases, which are called tauopathies. It was previously reported that, by cryo-electron microscopy, the structures of tau filaments from Alzheimer's disease, Pick's disease, chronic traumatic encephalopathy and corticobasal degeneration are distinct. Here we show that the structures of tau filaments from progressive supranuclear palsy (PSP) define a new three-layered fold. Moreover, the structures of tau filaments from globular glial tauopathy are similar to those from PSP. The tau filament fold of argyrophilic grain disease (AGD) differs, instead resembling the four-layered fold of corticobasal degeneration. The AGD fold is also observed in ageing-related tau astrogliopathy. Tau protofilament structures from inherited cases of mutations at positions +3 or +16 in intron 10 of MAPT (the microtubule-associated protein tau gene) are also identical to those from AGD, suggesting that relative overproduction of four-repeat tau can give rise to the AGD fold. Finally, the structures of tau filaments from cases of familial British dementia and familial Danish dementia are the same as those from cases of Alzheimer's disease and primary age-related tauopathy. These findings suggest a hierarchical classification of tauopathies on the basis of their filament folds, which complements clinical diagnosis and neuropathology and also allows the identification of new entities-as we show for a case diagnosed as PSP, but with filament structures that are intermediate between those of globular glial tauopathy and PSP. | |||||||||||||||||||||||||||||||||||||||
History |
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Structure visualization
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Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 219.4 KB | Display | ![]() |
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PDB format | ![]() | 164.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 13220MC ![]() 7p65C ![]() 7p66C ![]() 7p68C ![]() 7p6aC ![]() 7p6bC ![]() 7p6cC ![]() 7p6dC ![]() 7p6eC M: map data used to model this data C: citing same article ( |
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Similar structure data | |
EM raw data | ![]() Data size: 671.0 Data #1: Unaligned multi-frame movies [micrographs - multiframe]) |
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Links
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Assembly
Deposited unit | ![]()
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Components
#1: Protein | ![]() Mass: 45919.871 Da / Num. of mol.: 10 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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EM experiment | Aggregation state: HELICAL ARRAY / 3D reconstruction method: helical reconstruction |
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Sample preparation
Component | Name: Sarkosyl-insoluble fraction from the frontal cortex of an individual with Type I globular glial tauopathy Type: TISSUE / Entity ID: all / Source: NATURAL |
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Source (natural) | Organism: ![]() ![]() |
Buffer solution | pH: 7.4 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied![]() ![]() |
Vitrification![]() | Cryogen name: ETHANE |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source![]() ![]() |
Electron lens | Mode: BRIGHT FIELD![]() |
Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
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Processing
Software | Name: PHENIX / Version: 1.19.2_4158: / Classification: refinement | ||||||||||||||||||||||||
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CTF correction![]() | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
Helical symmerty | Angular rotation/subunit: 179.65 ° / Axial rise/subunit: 2.37 Å / Axial symmetry: C1 | ||||||||||||||||||||||||
3D reconstruction![]() | Resolution: 3.1 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 42381 / Symmetry type: HELICAL | ||||||||||||||||||||||||
Refine LS restraints |
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