› 7qki

Electron Microscopy
3.13Å resolution

In vitro assembled 297-408 S396D S400D T403D S404D tau filaments (42a)

Released:
DOI: 10.2210/pdb7qki/pdb
PDB entry 7qki coloured by chain, front view.
PDB entry 7qki coloured by chain, side view.
PDB entry 7qki coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Assembly of recombinant tau into filaments identical to those of Alzheimer's disease and chronic traumatic encephalopathy.
Lövestam S, Koh FA, van Knippenberg B, Kotecha A, Murzin AG, Goedert M, Scheres SHW
OpenAccess logo Elife 11 (2022)
PMID: 35244536
Related structures: EMD-14043

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-536101 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Microtubule-associated protein tau Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 441 amino acids
Theoretical weight: 45.92 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P10636 (Residues: 1-758; Coverage: 58%)
  • Best match: P10636-8 (Residues: 1-441)
Gene names: MAPT, MAPTL, MTBT1, TAU
Sequence domains: Tau and MAP protein, tubulin-binding repeat

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.13Å
Relevant EMDB volumes: EMD-14043
Expression system: Escherichia coli

Quick links

Citations

24 review citations

Molecular pathology of neurodegenerative diseases by cryo-EM of amyloids.
Scheres et al. (2023)
23 more

1 mention without citation

Insights into the Structural Conformations of the Tau Protein in Different Aggregation Status.
Pinzi et al. (2023)