Fig. 3: Cryo-EM structure of the Ac-E46K α-syn fibril. | Nature Communications

Fig. 3: Cryo-EM structure of the Ac-E46K α-syn fibril.

From: Parkinson’s disease associated mutation E46K of α-synuclein triggers the formation of a distinct fibril structure

Fig. 3

a Top view of the Ac-E46K fibril. One layer of the structure is shown, which consists of two α-syn molecules covering residues 45–99. The two molecules are colored differently. b Views of six layers of the Ac-E46K fibril are shown in cartoon. The two protofilaments are colored differently. The fibril axis is indicated. The β strands are numbered and labeled. c Overlay of the α-syn subunit structures of the Ac-E46K and Ac-WT fibrils. The two structures diverge mainly at the FC-N region. The interfaces between the FC-N and FC-C regions are shown in the zoom-in views. The residues involved in the interfaces are labeled and their side chains are shown in spheres. d Comparison of the FC-C region of the Ac-E46K and Ac-WT fibrils. Five layers of a single protofilament is shown. The structures are colored by different layers. The FC-C region adopts similar topology in the two structures, while their structural arrangements in the two fibrils are markedly different. The FC-C of the Ac-WT fibril folds in a flat layer. In contrast, in the Ac-E46K fibril, β6 and β7 swap to the next α-syn molecule in the neighboring layer.

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