期刊
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
卷 467, 期 2, 页码 239-248出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2007.08.010
关键词
electron microscopy; immunolabeling; two-dimensional crystals; miniprion; uranyl binding; ammonium molybdate
资金
- NIA NIH HHS [P01 AG002132-190001, P01 AG010770, P01 AG021601-01, P01 AG021601, AG021601, AG02132, P01 AG010770-07, AG10770, P01 AG002132] Funding Source: Medline
The insolubility of the disease-causing isoform of the prion protein (PrPsc) has prevented studies of its three-dimensional structure at atomic resolution. Electron crystallography of two-dimensional crystals of N-terminally truncated PrPsc (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 PrPsc. Differential staining also confirmed the location of the internal deletion of PrP(sc)106 at or near these densities. (C) 2007 Elsevier Inc. All rights reserved.
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