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TitleCryo-EM structure of a novel α-synuclein filament subtype from multiple system atrophy.
Journal, issue, pagesFEBS Lett, Vol. 599, Issue 1, Page 33-40, Year 2025
Publish dateNov 7, 2024
AuthorsNicholas L Yan / Francisco Candido / Eric Tse / Arthur A Melo / Stanley B Prusiner / Daniel A Mordes / Daniel R Southworth / Nick A Paras / Gregory E Merz /
PubMed AbstractMultiple system atrophy (MSA) is a progressive neurodegenerative disease characterized by accumulation of α-synuclein cross-β amyloid filaments in the brain. Previous structural studies of these ...Multiple system atrophy (MSA) is a progressive neurodegenerative disease characterized by accumulation of α-synuclein cross-β amyloid filaments in the brain. Previous structural studies of these filaments by cryo-electron microscopy (cryo-EM) revealed three discrete folds distinct from α-synuclein filaments associated with other neurodegenerative diseases. Here, we use cryo-EM to identify a novel, low-populated MSA filament subtype (designated Type I) in addition to a predominant class comprising MSA Type II filaments. The 3.3-Å resolution structure of the Type I filament reveals a fold consisting of two asymmetric protofilaments, one of which adopts a novel structure that is chimeric between two previously reported protofilaments. These results further define MSA-specific folds of α-synuclein filaments and have implications for designing MSA diagnostics and therapeutics.
External linksFEBS Lett / PubMed:39511911 / PubMed Central
MethodsEM (helical sym.)
Resolution3.2 - 3.3 Å
Structure data

45464

9cd9

EMDB-45464, PDB-9cd9:
Structure of type II-2 alpha-synuclein filament from multiple system atrophy
Method: EM (helical sym.) / Resolution: 3.2 Å

45465

9cda

EMDB-45465, PDB-9cda:
Structure of type I-2 alpha-synuclein filament from multiple system atrophy
Method: EM (helical sym.) / Resolution: 3.3 Å

Source
  • homo sapiens (human)
KeywordsPROTEIN FIBRIL / fibril / synuclein

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