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TitleParkinson's disease associated mutation E46K of α-synuclein triggers the formation of a distinct fibril structure.
Journal, issue, pagesNat Commun, Vol. 11, Issue 1, Page 2643, Year 2020
Publish dateMay 26, 2020
AuthorsKun Zhao / Yaowang Li / Zhenying Liu / Houfang Long / Chunyu Zhao / Feng Luo / Yunpeng Sun / Youqi Tao / Xiao-Dong Su / Dan Li / Xueming Li / Cong Liu /
PubMed AbstractAmyloid aggregation of α-synuclein (α-syn) is closely associated with Parkinson's disease (PD) and other synucleinopathies. Several single amino-acid mutations (e.g. E46K) of α-syn have been ...Amyloid aggregation of α-synuclein (α-syn) is closely associated with Parkinson's disease (PD) and other synucleinopathies. Several single amino-acid mutations (e.g. E46K) of α-syn have been identified causative to the early onset of familial PD. Here, we report the cryo-EM structure of an α-syn fibril formed by N-terminally acetylated E46K mutant α-syn (Ac-E46K). The fibril structure represents a distinct fold of α-syn, which demonstrates that the E46K mutation breaks the electrostatic interactions in the wild type (WT) α-syn fibril and thus triggers the rearrangement of the overall structure. Furthermore, we show that the Ac-E46K fibril is less resistant to harsh conditions and protease cleavage, and more prone to be fragmented with an enhanced seeding capability than that of the WT fibril. Our work provides a structural view to the severe pathology of the PD familial mutation E46K of α-syn and highlights the importance of electrostatic interactions in defining the fibril polymorphs.
External linksNat Commun / PubMed:32457390 / PubMed Central
MethodsEM (helical sym.)
Resolution3.37 Å
Structure data

0833

6l4s

EMDB-0833, PDB-6l4s:
cryo-em structure of alpha-synuclein fiber mutation type E46K
Method: EM (helical sym.) / Resolution: 3.37 Å

Source
  • homo sapiens (human)
KeywordsPROTEIN FIBRIL / alpha-syn fiber / Parkinson disease

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