Sub-ångström cryo-EM structure of a prion protofibril reveals a polar clasp.
Marcus Gallagher-JonesCalina GlynnDavid R BoyerMichael W MartynowyczEvelyn HernandezJennifer MiaoChih-Te ZeeIrina V NovikovaLukasz GoldschmidtHeather T McFarlaneGustavo F HelgueraJames E EvansMichael R SawayaDuilio CascioDavid S EisenbergTamir GonenJosé A RodriguezPublished in: Nature structural & molecular biology (2018)
The atomic structure of the infectious, protease-resistant, β-sheet-rich and fibrillar mammalian prion remains unknown. Through the cryo-EM method MicroED, we reveal the sub-ångström-resolution structure of a protofibril formed by a wild-type segment from the β2-α2 loop of the bank vole prion protein. The structure of this protofibril reveals a stabilizing network of hydrogen bonds that link polar zippers within a sheet, producing motifs we have named 'polar clasps'.