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TitleAmyloid fibril structure of α-synuclein determined by cryo-electron microscopy.
Journal, issue, pagesCell Res, Vol. 28, Issue 9, Page 897-903, Year 2018
Publish dateJul 31, 2018
AuthorsYaowang Li / Chunyu Zhao / Feng Luo / Zhenying Liu / Xinrui Gui / Zhipu Luo / Xiang Zhang / Dan Li / Cong Liu / Xueming Li /
PubMed Abstractα-Synuclein (α-syn) amyloid fibrils are the major component of Lewy bodies, which are the pathological hallmark of Parkinson's disease (PD) and other synucleinopathies. High-resolution structure of ...α-Synuclein (α-syn) amyloid fibrils are the major component of Lewy bodies, which are the pathological hallmark of Parkinson's disease (PD) and other synucleinopathies. High-resolution structure of α-syn fibril is important for understanding its assembly and pathological mechanism. Here, we determined a fibril structure of full-length α-syn (1-140) at the resolution of 3.07 Å by cryo-electron microscopy (cryo-EM). The fibrils are cytotoxic, and transmissible to induce endogenous α-syn aggregation in primary neurons. Based on the reconstructed cryo-EM density map, we were able to unambiguously build the fibril structure comprising residues 37-99. The α-syn amyloid fibril structure shows two protofilaments intertwining along an approximate 2 screw axis into a left-handed helix. Each protofilament features a Greek key-like topology. Remarkably, five out of the six early-onset PD familial mutations are located at the dimer interface of the fibril (H50Q, G51D, and A53T/E) or involved in the stabilization of the protofilament (E46K). Furthermore, these PD mutations lead to the formation of fibrils with polymorphic structures distinct from that of the wild-type. Our study provides molecular insight into the fibrillar assembly of α-syn at the atomic level and sheds light on the molecular pathogenesis caused by familial PD mutations of α-syn.
External linksCell Res / PubMed:30065316 / PubMed Central
MethodsEM (helical sym.)
Resolution3.07 Å
Structure data

6988

6a6b

EMDB-6988, PDB-6a6b:
cryo-em structure of alpha-synuclein fiber
Method: EM (helical sym.) / Resolution: 3.07 Å

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

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