8R4A
Cryo-EM structure of the D87G lysozyme amyloid fibril
Summary for 8R4A
| Entry DOI | 10.2210/pdb8r4a/pdb |
| EMDB information | 18883 |
| Descriptor | Lysozyme C (1 entity in total) |
| Functional Keywords | lysozyme, amyloid fibril, misfolding disease, cryo-em, alys amyloidosis, amyloidogenic variant, protein fibril |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 9 |
| Total formula weight | 131963.92 |
| Authors | Karimi-Farsijani, S.,Sharma, K.,Schmidt, M.,Faendrich, M. (deposition date: 2023-11-13, release date: 2024-11-20, Last modification date: 2024-11-27) |
| Primary citation | Karimi-Farsijani, S.,Sharma, K.,Ugrina, M.,Kuhn, L.,Pfeiffer, P.B.,Haupt, C.,Wiese, S.,Hegenbart, U.,Schonland, S.O.,Schwierz, N.,Schmidt, M.,Fandrich, M. Cryo-EM structure of a lysozyme-derived amyloid fibril from hereditary amyloidosis. Nat Commun, 15:9648-9648, 2024 Cited by PubMed Abstract: Systemic ALys amyloidosis is a debilitating protein misfolding disease that arises from the formation of amyloid fibrils from C-type lysozyme. We here present a 2.8 Å cryo-electron microscopy structure of an amyloid fibril, which was isolated from the abdominal fat tissue of a patient who expressed the D87G variant of human lysozyme. We find that the fibril possesses a stable core that is formed by all 130 residues of the fibril precursor protein. There are four disulfide bonds in each fibril protein that connect the same residues as in the globularly folded protein. As the conformation of lysozyme in the fibril is otherwise fundamentally different from native lysozyme, our data provide a structural rationale for the need of protein unfolding in the development of systemic ALys amyloidosis. PubMed: 39511224DOI: 10.1038/s41467-024-54091-7 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.8 Å) |
Structure validation
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