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TitleTwo new polymorphic structures of human full-length alpha-synuclein fibrils solved by cryo-electron microscopy.
Journal, issue, pagesElife, Vol. 8, Year 2019
Publish dateDec 9, 2019
AuthorsRicardo Guerrero-Ferreira / Nicholas Mi Taylor / Ana-Andreea Arteni / Pratibha Kumari / Daniel Mona / Philippe Ringler / Markus Britschgi / Matthias E Lauer / Ali Makky / Joeri Verasdonck / Roland Riek / Ronald Melki / Beat H Meier / Anja Böckmann / Luc Bousset / Henning Stahlberg /
PubMed AbstractIntracellular inclusions rich in alpha-synuclein are a hallmark of several neuropathological diseases including Parkinson's disease (PD). Previously, we reported the structure of alpha-synuclein ...Intracellular inclusions rich in alpha-synuclein are a hallmark of several neuropathological diseases including Parkinson's disease (PD). Previously, we reported the structure of alpha-synuclein fibrils (residues 1-121), composed of two protofibrils that are connected via a densely-packed interface formed by residues 50-57 (Guerrero-Ferreira, eLife 218;7:e36402). We here report two new polymorphic atomic structures of alpha-synuclein fibrils termed polymorphs 2a and 2b, at 3.0 Å and 3.4 Å resolution, respectively. These polymorphs show a radically different structure compared to previously reported polymorphs. The new structures have a 10 nm fibril diameter and are composed of two protofilaments which interact via intermolecular salt-bridges between amino acids K45, E57 (polymorph 2a) or E46 (polymorph 2b). The non-amyloid component (NAC) region of alpha-synuclein is fully buried by previously non-described interactions with the N-terminus. A hydrophobic cleft, the location of familial PD mutation sites, and the nature of the protofilament interface now invite to formulate hypotheses about fibril formation, growth and stability.
External linksElife / PubMed:31815671 / PubMed Central
MethodsEM (helical sym.)
Resolution2.98 - 3.46 Å
Structure data

10305

6sst

EMDB-10305, PDB-6sst:
cryo-em structure of alpha-synuclein fibril polymorph 2B
Method: EM (helical sym.) / Resolution: 3.4 Å

10307

6ssx

EMDB-10307, PDB-6ssx:
cryo-em structure of alpha-synuclein fibril polymorph 2A
Method: EM (helical sym.) / Resolution: 2.98 Å

4994

6rt0

EMDB-4994: cryo-em of alpha-synuclein fibril polymorph 2A
PDB-6rt0: cryo-em structure of alpha-synuclein fibril polymorph 2A
Method: EM (helical sym.) / Resolution: 3.1 Å

4996

6rtb

EMDB-4996, PDB-6rtb:
cryo-em structure of alpha-synuclein fibril polymorph 2B
Method: EM (helical sym.) / Resolution: 3.46 Å

Source
  • homo sapiens (human)
KeywordsPROTEIN FIBRIL / amyloid / parkinson

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