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TitleAtomic structure and hierarchical assembly of a cross-β amyloid fibril.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 110, Issue 14, Page 5468-5473, Year 2013
Publish dateApr 2, 2013
AuthorsAnthony W P Fitzpatrick / Galia T Debelouchina / Marvin J Bayro / Daniel K Clare / Marc A Caporini / Vikram S Bajaj / Christopher P Jaroniec / Luchun Wang / Vladimir Ladizhansky / Shirley A Müller / Cait E MacPhee / Christopher A Waudby / Helen R Mott / Alfonso De Simone / Tuomas P J Knowles / Helen R Saibil / Michele Vendruscolo / Elena V Orlova / Robert G Griffin / Christopher M Dobson /
PubMed AbstractThe cross-β amyloid form of peptides and proteins represents an archetypal and widely accessible structure consisting of ordered arrays of β-sheet filaments. These complex aggregates have ...The cross-β amyloid form of peptides and proteins represents an archetypal and widely accessible structure consisting of ordered arrays of β-sheet filaments. These complex aggregates have remarkable chemical and physical properties, and the conversion of normally soluble functional forms of proteins into amyloid structures is linked to many debilitating human diseases, including several common forms of age-related dementia. Despite their importance, however, cross-β amyloid fibrils have proved to be recalcitrant to detailed structural analysis. By combining structural constraints from a series of experimental techniques spanning five orders of magnitude in length scale--including magic angle spinning nuclear magnetic resonance spectroscopy, X-ray fiber diffraction, cryoelectron microscopy, scanning transmission electron microscopy, and atomic force microscopy--we report the atomic-resolution (0.5 Å) structures of three amyloid polymorphs formed by an 11-residue peptide. These structures reveal the details of the packing interactions by which the constituent β-strands are assembled hierarchically into protofilaments, filaments, and mature fibrils.
External linksProc Natl Acad Sci U S A / PubMed:23513222 / PubMed Central
MethodsEM (single particle) / NMR (solid-state)
Resolution11.6 - 12.7 Å
Structure data

2323

2m5m

EMDB-2323: Electron cryo-microscopy of a cross-beta amyloid fibril polymorph
PDB-2m5m: Atomic-resolution structure of a triplet cross-beta amyloid fibril
Method: EM (single particle) / Resolution: 12.2 Å

2324

3zpk

EMDB-2324: Electron cryo-microscopy of a cross-beta amyloid fibril polymorph
PDB-3zpk: Atomic-resolution structure of a quadruplet cross-beta amyloid fibril.
Method: EM (single particle) / Resolution: 11.6 Å

5590

2m5k

EMDB-5590: Electron cryo-microscopy of a cross-beta amyloid fibril polymorph
PDB-2m5k: Atomic-resolution structure of a doublet cross-beta amyloid fibril
Method: EM (single particle) / Resolution: 12.7 Å

PDB-2m5n:
Atomic-resolution structure of a cross-beta protofilament
Method: SOLID-STATE NMR

Source
  • rattus norvegicus (Norway rat)
  • homo sapiens (human)
KeywordsPROTEIN FIBRIL / amyloid fibril / cross-beta structure

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