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TitleCryo-EM structure of a lysozyme-derived amyloid fibril from hereditary amyloidosis.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 9648, Year 2024
Publish dateNov 7, 2024
AuthorsSara Karimi-Farsijani / Kartikay Sharma / Marijana Ugrina / Lukas Kuhn / Peter Benedikt Pfeiffer / Christian Haupt / Sebastian Wiese / Ute Hegenbart / Stefan O Schönland / Nadine Schwierz / Matthias Schmidt / Marcus Fändrich /
PubMed AbstractSystemic 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 ...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.
External linksNat Commun / PubMed:39511224 / PubMed Central
MethodsEM (helical sym.)
Resolution2.8 Å
Structure data

18883

8r4a

EMDB-18883, PDB-8r4a:
Cryo-EM structure of the D87G lysozyme amyloid fibril
Method: EM (helical sym.) / Resolution: 2.8 Å

Source
  • homo sapiens (human)
KeywordsPROTEIN FIBRIL / Lysozyme / amyloid fibril / misfolding disease / cryo-EM / ALys amyloidosis / amyloidogenic variant

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