› 6lrq

Electron Microscopy
3.49Å resolution

Cryo-EM structure of A53T alpha-synuclein amyloid fibril

Released:
DOI: 10.2210/pdb6lrq/pdb
PDB entry 6lrq coloured by chain, front view.
PDB entry 6lrq coloured by chain, side view.
PDB entry 6lrq coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Cryo-EM structure of full-length α-synuclein amyloid fibril with Parkinson's disease familial A53T mutation.
Sun Y, Hou S, Zhao K, Long H, Liu Z, Gao J, Zhang Y, Su XD, Li D, Liu C
Cell Res 30 360-362 (2020)
PMID: 32203130
Related structures: EMD-0958

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153511 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-synuclein Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 140 amino acids
Theoretical weight: 14.51 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P37840 (Residues: 1-140; Coverage: 100%)
Gene names: NACP, PARK1, SNCA
Sequence domains: Synuclein

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.49Å
Relevant EMDB volumes: EMD-0958
Expression system: Escherichia coli

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Citations

12 review citations

Interaction of Alpha-Synuclein With Lipids: Mitochondrial Cardiolipin as a Critical Player in the Pathogenesis of Parkinson's Disease.
Gilmozzi et al. (2020)
11 more

9 mentions without citation

Neuropathology and molecular diagnosis of Synucleinopathies.
Koga et al. (2021)
8 more