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TitleCryo-EM fibril structures from systemic AA amyloidosis reveal the species complementarity of pathological amyloids.
Journal, issue, pagesNat Commun, Vol. 10, Issue 1, Page 1104, Year 2019
Publish dateMar 7, 2019
AuthorsFalk Liberta / Sarah Loerch / Matthies Rennegarbe / Angelika Schierhorn / Per Westermark / Gunilla T Westermark / Bouke P C Hazenberg / Nikolaus Grigorieff / Marcus Fändrich / Matthias Schmidt /
PubMed AbstractSystemic AA amyloidosis is a worldwide occurring protein misfolding disease of humans and animals. It arises from the formation of amyloid fibrils from the acute phase protein serum amyloid A. Here, ...Systemic AA amyloidosis is a worldwide occurring protein misfolding disease of humans and animals. It arises from the formation of amyloid fibrils from the acute phase protein serum amyloid A. Here, we report the purification and electron cryo-microscopy analysis of amyloid fibrils from a mouse and a human patient with systemic AA amyloidosis. The obtained resolutions are 3.0 Å and 2.7 Å for the murine and human fibril, respectively. The two fibrils differ in fundamental properties, such as presence of right-hand or left-hand twisted cross-β sheets and overall fold of the fibril proteins. Yet, both proteins adopt highly similar β-arch conformations within the N-terminal ~21 residues. Our data demonstrate the importance of the fibril protein N-terminus for the stability of the analyzed amyloid fibril morphologies and suggest strategies of combating this disease by interfering with specific fibril polymorphs.
External linksPubMed:30846696 / Publisher's page
KeywordsAmino Acid Sequence / Amyloid / Amyloidosis / Animals / Cryoelectron Microscopy / Female / Humans / Mice / Microscopy, Electron, Transmission / Middle Aged / Models, Molecular / Protein Conformation / Protein Conformation, beta-Strand / Protein Interaction Domains and Motifs / Protein Stability / Sequence Homology, Amino Acid / Serum Amyloid A Protein / Species Specificity / PROTEIN FIBRIL / AA-amyloidosis / fibril / cross-beta / helical / Serum Amyloid A
MethodsEM (helical sym.)
Resolution2.7 - 3 A
Structure data

EMDB-8910:
Cryo-EM structure of murine AA amyloid fibril

EMDB-9232:
Cryo-EM structure of human AA amyloid fibril

PDB-6dso:
Cryo-EM structure of murine AA amyloid fibril

PDB-6mst:
Cryo-EM structure of human AA amyloid fibril

Source
  • mus musculus (house mouse)
  • Mouse (mice)
  • homo sapiens (human)
  • Human (human)

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    • Jacques Dubochet (University of Lausanne, Switzerland) is a pioneer of ice-embedding method of EM specimen (as known as cryo-EM), Most of 3DEM structures in EMDB and PDB are obtained using his method.
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