Fibrils of the hamster prion peptide (sHaPrP, sequence
108–144)
were prepared in an acidic solution, and their structure was solved
by cryogenic electron microscopy with a resolution of 2.23 Å
based on the gold-standard Fourier shell correlation (FSC) curve.
The fibril has a novel architecture that has never been found in other
amyloid fibrils. Each fibril is assembled by four protofilaments (PFs)
and has an ordered water channel in the center. Each protofilament
contains three β-strands (125–130, 133–135, and
138–141) arranged in an “R”-shaped construct.
The structural data indicate that these three β-strand segments
are the most amyloidogenic region of the prion peptide/protein and
might be the site of nucleation during fibrillization under conditions
without denaturants.
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