7TD6

aRML prion fibril

Summary for 7TD6

• Entry DOI: 10.2210/pdb7td6/pdb
• EMDB information: 25824
• Descriptor: Major prion protein (1 entity in total)
• Functional Keywords: infectious prion, protein fibril, amyloid, parallel in-register
• Biological source: Mus musculus (house mouse)
• Total number of polymer chains: 5
• Total formula weight: 140041.96

Authors

Hoyt, F.,Standke, H.G.,Artikis, E.,Caughey, B.,Kraus, A. (deposition date: 2021-12-30, release date: 2022-07-20, Last modification date: 2024-10-30)

Primary citation

Hoyt, F.,Standke, H.G.,Artikis, E.,Schwartz, C.L.,Hansen, B.,Li, K.,Hughson, A.G.,Manca, M.,Thomas, O.R.,Raymond, G.J.,Race, B.,Baron, G.S.,Caughey, B.,Kraus, A.
Cryo-EM structure of anchorless RML prion reveals variations in shared motifs between distinct strains.
Nat Commun, 13:4005-4005, 2022

PubMed Abstract: Little is known about the structural basis of prion strains. Here we provide a high (3.0 Å) resolution cryo-electron microscopy-based structure of infectious brain-derived fibrils of the mouse anchorless RML scrapie strain which, like the recently determined hamster 263K strain, has a parallel in-register β-sheet-based core. Several structural motifs are shared between these ex vivo prion strains, including an amino-proximal steric zipper and three β-arches. However, detailed comparisons reveal variations in these shared structural topologies and other features. Unlike 263K and wildtype RML prions, the anchorless RML prions lack glycophosphatidylinositol anchors and are severely deficient in N-linked glycans. Nonetheless, the similarity of our anchorless RML structure to one reported for wildtype RML prion fibrils in an accompanying paper indicates that these post-translational modifications do not substantially alter the amyloid core conformation. This work demonstrates both common and divergent structural features of prion strains at the near-atomic level.

PubMed: 35831291
DOI: 10.1038/s41467-022-30458-6

Experimental method

ELECTRON MICROSCOPY (3 Å)