5OQV

Near-atomic resolution fibril structure of complete amyloid-beta(1-42) by cryo-EM

Summary for 5OQV

• Entry DOI: 10.2210/pdb5oqv/pdb
• EMDB information: 3851
• NMR Information: BMRB: 27212
• Descriptor: Amyloid beta A4 protein (1 entity in total)
• Functional Keywords: amyloid, fibril, aggregation, alzheimer's disease, protein fibril
• Biological source: Homo sapiens (Human)
• Cellular location: Membrane; Single-pass type I membrane protein: P05067
• Total number of polymer chains: 9
• Total formula weight: 40680.78

Authors

Gremer, L.,Schoelzel, D.,Schenk, C.,Reinartz, E.,Labahn, J.,Ravelli, R.,Tusche, M.,Lopez-Iglesias, C.,Hoyer, W.,Heise, H.,Willbold, D.,Schroeder, G.F. (deposition date: 2017-08-14, release date: 2017-09-13, Last modification date: 2024-05-15)

Primary citation

Gremer, L.,Scholzel, D.,Schenk, C.,Reinartz, E.,Labahn, J.,Ravelli, R.B.G.,Tusche, M.,Lopez-Iglesias, C.,Hoyer, W.,Heise, H.,Willbold, D.,Schroder, G.F.
Fibril structure of amyloid-beta (1-42) by cryo-electron microscopy.
Science, 358:116-119, 2017

PubMed Abstract: Amyloids are implicated in neurodegenerative diseases. Fibrillar aggregates of the amyloid-β protein (Aβ) are the main component of the senile plaques found in brains of Alzheimer's disease patients. We present the structure of an Aβ(1-42) fibril composed of two intertwined protofilaments determined by cryo-electron microscopy (cryo-EM) to 4.0-angstrom resolution, complemented by solid-state nuclear magnetic resonance experiments. The backbone of all 42 residues and nearly all side chains are well resolved in the EM density map, including the entire N terminus, which is part of the cross-β structure resulting in an overall "LS"-shaped topology of individual subunits. The dimer interface protects the hydrophobic C termini from the solvent. The characteristic staggering of the nonplanar subunits results in markedly different fibril ends, termed "groove" and "ridge," leading to different binding pathways on both fibril ends, which has implications for fibril growth.

PubMed: 28882996
DOI: 10.1126/science.aao2825

Experimental method

ELECTRON MICROSCOPY (4 Å)