7ZH7
Cryo-EM structure of ex vivo AA amyloid from renal tissue of a short hair cat deceased in a shelter
Summary for 7ZH7
Entry DOI | 10.2210/pdb7zh7/pdb |
EMDB information | 14726 |
Descriptor | Serum amyloid A protein (1 entity in total) |
Functional Keywords | aa amyloidosis, cat, serum amyloid a, protein fibril |
Biological source | Felis catus (domestic cat) |
Total number of polymer chains | 10 |
Total formula weight | 144497.66 |
Authors | Schulte, T.,Chaves-Sanjuan, A.,Ricagno, S. (deposition date: 2022-04-05, release date: 2022-11-30, Last modification date: 2024-07-24) |
Primary citation | Schulte, T.,Chaves-Sanjuan, A.,Mazzini, G.,Speranzini, V.,Lavatelli, F.,Ferri, F.,Palizzotto, C.,Mazza, M.,Milani, P.,Nuvolone, M.,Vogt, A.C.,Vogel, M.,Palladini, G.,Merlini, G.,Bolognesi, M.,Ferro, S.,Zini, E.,Ricagno, S. Cryo-EM structure of ex vivo fibrils associated with extreme AA amyloidosis prevalence in a cat shelter. Nat Commun, 13:7041-7041, 2022 Cited by PubMed Abstract: AA amyloidosis is a systemic disease characterized by deposition of misfolded serum amyloid A protein (SAA) into cross-β amyloid in multiple organs in humans and animals. AA amyloidosis occurs at high SAA serum levels during chronic inflammation. Prion-like transmission was reported as possible cause of extreme AA amyloidosis prevalence in captive animals, e.g. 70% in cheetah and 57-73% in domestic short hair (DSH) cats kept in zoos and shelters, respectively. Herein, we present the 3.3 Å cryo-EM structure of AA amyloid extracted post-mortem from the kidney of a DSH cat with renal failure, deceased in a shelter with extreme disease prevalence. The structure reveals a cross-β architecture assembled from two 76-residue long proto-filaments. Despite >70% sequence homology to mouse and human SAA, the cat SAA variant adopts a distinct amyloid fold. Inclusion of an eight-residue insert unique to feline SAA contributes to increased amyloid stability. The presented feline AA amyloid structure is fully compatible with the 99% identical amino acid sequence of amyloid fragments of captive cheetah. PubMed: 36396658DOI: 10.1038/s41467-022-34743-2 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.3 Å) |
Structure validation
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