Electron crystallography of the scrapie prion protein complexed with heavy metals.
Arch Biochem Biophys
; 467(2): 239-48, 2007 Nov 15.
Article
em En
| MEDLINE
| ID: mdl-17935686
ABSTRACT
The insolubility of the disease-causing isoform of the prion protein (PrP(Sc)) has prevented studies of its three-dimensional structure at atomic resolution. Electron crystallography of two-dimensional crystals of N-terminally truncated PrP(Sc) (PrP 27-30) and a miniprion (PrP(Sc)106) provided the first insights at intermediate resolution on the molecular architecture of the prion. Here, we report on the structure of PrP 27-30 and PrP(Sc)106 negatively stained with heavy metals. The interactions of the heavy metals with the crystal lattice were governed by tertiary and quaternary structural elements of the protein as well as the charge and size of the heavy metal salts. Staining with molybdate anions revealed three prominent densities near the center of the trimer that forms the unit cell, coinciding with the location of the beta-helix that was proposed for the structure of PrP(Sc). Differential staining also confirmed the location of the internal deletion of PrP(Sc)106 at or near these densities.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Microscopia Eletrônica
/
Modelos Moleculares
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Proteínas PrPSc
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Metais Pesados
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Cristalografia
Idioma:
En
Revista:
Arch Biochem Biophys
Ano de publicação:
2007
Tipo de documento:
Article
País de afiliação:
Estados Unidos