Accession Number:

ADA282251

Title:

Structure and Stability of Pertussis Toxin Studied by the Situ Atomic Force Microscopy

Descriptive Note:

Corporate Author:

VIRGINIA UNIV CHARLOTTESVILLE

Personal Author(s):

Report Date:

1994-01-01

Pagination or Media Count:

5.0

Abstract:

Pertussis toxin, both complete and the B-oligomer, were imaged by atomic force microscopy AFM, using specimens prepared by simple surface adsorption on mica without further manipulation. The spatial arrangement of the subunits of the B-oligomer was clearly resolved, representing the first protein quaternary structure obtained by AFM in situ, The results suggest that the B- oligomer is a flat pentamer with the two large subunits located next to each other, and the catalytic A-subunit situated at the center above. We found that the B-pentamer was structurally stable for temperatures up to 60 deg C and within the pH range of 4.5-9.5. It is also demonstrated that the AFM was capable of resolving features down to 0.5 nm on the B-oligomers, indicating its great potential for structural determination.

Subject Categories:

  • Biochemistry
  • Genetic Engineering and Molecular Biology
  • Microbiology

Distribution Statement:

APPROVED FOR PUBLIC RELEASE