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TitleSub-ångström cryo-EM structure of a prion protofibril reveals a polar clasp.
Journal, issue, pagesNat Struct Mol Biol, Vol. 25, Issue 2, Page 131-134, Year 2018
Publish dateJan 15, 2018
AuthorsMarcus Gallagher-Jones / Calina Glynn / David R Boyer / Michael W Martynowycz / Evelyn Hernandez / Jennifer Miao / Chih-Te Zee / Irina V Novikova / Lukasz Goldschmidt / Heather T McFarlane / Gustavo F Helguera / James E Evans / Michael R Sawaya / Duilio Cascio / David S Eisenberg / Tamir Gonen / Jose A Rodriguez /
PubMed AbstractThe atomic structure of the infectious, protease-resistant, β-sheet-rich and fibrillar mammalian prion remains unknown. Through the cryo-EM method MicroED, we reveal the sub-ångström-resolution ...The atomic structure of the infectious, protease-resistant, β-sheet-rich and fibrillar mammalian prion remains unknown. Through the cryo-EM method MicroED, we reveal the sub-ångström-resolution structure of a protofibril formed by a wild-type segment from the β2-α2 loop of the bank vole prion protein. The structure of this protofibril reveals a stabilizing network of hydrogen bonds that link polar zippers within a sheet, producing motifs we have named 'polar clasps'.
External linksNat Struct Mol Biol / PubMed:29335561 / PubMed Central
MethodsEM (electron crystallography) / X-ray diffraction
Resolution0.75 - 1.1 Å
Structure data

7017

6axz

EMDB-7017, PDB-6axz:
Segment from bank vole prion protein 168-176 QYNNQNNFV
Method: EM (electron crystallography)

EMDB-7287:
MicroED structure of carbamazepine at 0.85 A resolution
Method: EM (electron crystallography) / Resolution: 0.85 Å

PDB-6btk:
Segment from bank vole prion protein 168-176 QYNNQNNFV
Method: X-RAY DIFFRACTION / Resolution: 1.1 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • myodes glareolus (Bank vole)
  • unidentified (others)
KeywordsPROTEIN FIBRIL / polar clasp / amyloid fibril / prion

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