Fig. 4: Rearrangement of the α-syn fibril structure triggered by E46K mutation. | Nature Communications

Fig. 4: Rearrangement of the α-syn fibril structure triggered by E46K mutation.

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

Fig. 4

a Electrostatic interactions in the Ac-WT and Ac-E46K fibrils. K/E pairs that form salt bridges are highlighted with spheres and shown in zoom-in views in (b). The FC-N region (residues 37/45–59) is colored in orange. The mutation site E46/K46 is highlighted in red/blue. The black solid ellipses in all panels indicate the symmetric axis of the dimeric α-syn structure. b Zoom-in views of the corresponding regions in (a). Distances of the electrostatic interactions are indicated, and involved residues are labeled. The mutation site E46 is highlighted in red. c Protofilamental interfaces of the Ac-WT and Ac-E46K fibrils. Residues involved in the interfaces are highlighted with spheres. The fibril interface of Ac-WT fibril is colored in yellow; that of the Ac-E46K fibril is in blue. The interfaces are zoomed in (d). d Zoom-in views of the fibril interfaces. Interface residues are labeled. e Conformational change of the FC-N region results in a decreased stability of this region. Three layers of the α-syn fibrils are shown in B-factor putty. The FC-N region is shown in lines and highlighted with orange ellipses.

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