8Y2P
The cryo-EM structure of a-synuclein fibril in Tris buffer.
Summary for 8Y2P
| Entry DOI | 10.2210/pdb8y2p/pdb |
| EMDB information | 38862 |
| Descriptor | Alpha-synuclein (1 entity in total) |
| Functional Keywords | amyloid, protein fibril |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 6 |
| Total formula weight | 86856.65 |
| Authors | Yao, Y.X.,Zhao, Q.Y.,Liu, C.,Li, D. (deposition date: 2024-01-27, release date: 2025-01-29, Last modification date: 2026-02-18) |
| Primary citation | Yao, Y.,Zhao, Q.,Tao, Y.,Liu, K.,Cao, T.,Chen, Z.,Liu, C.,Le, W.,Zhao, J.,Li, D.,Kang, W. Different charged biopolymers induce alpha-synuclein to form fibrils with distinct structures. J.Biol.Chem., 300:107862-107862, 2024 Cited by PubMed Abstract: The aggregation of α-synuclein (α-syn) into amyloid fibrils, a key process in the development of Parkinson's disease (PD) and other synucleinopathies, is influenced by a range of factors such as charged biopolymers, chaperones, and metabolites. However, the specific impacts of different biopolymers on α-syn fibril structure are not well understood. In our work, we found that different polyanions and polycations, such as polyphosphate (polyP), polyuridine (polyU), and polyamines (including putrescine, spermidine, and spermine), markedly altered the fibrillation kinetics of α-syn in vitro. Furthermore, the seeding assay revealed distinct cross-seeding capacities across different biopolymer-induced α-syn fibrils, suggesting the formation of structurally distinct strains under different conditions. Utilizing cryo-electron microscopy (cryo-EM), we further examined the detailed structural configuration of α-syn fibrils formed in the presence of these biopolymers. Notably, we found that while polyamines do not change the atomic structure of α-syn fibrils, polyU and polyP induce the formation of distinct amyloid fibrils, exhibiting a range of structural polymorphs. Our work offers valuable insights into how various charged biopolymers affect the aggregation process and the resultant structures of α-syn fibrils, thereby enhancing our understanding of the structural variations in α-syn fibrils across different pathological conditions. PubMed: 39374778DOI: 10.1016/j.jbc.2024.107862 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.2 Å) |
Structure validation
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