Structure and stability of pertussis toxin studied by in situ atomic force microscopy

FEBS Letters

Shao, Zhifeng¹  Mou, Jianxun¹  Yang, Jie¹ 

[1]Bio-SPM Laboratory, Department of Molecular Physiology & Biological Physics and Biophysics Program, University of Virginia, Box 449, Charlottesville, VA 22908, USA

关键词: Atomic force microscopy;    Pertussis toxin;    Structure;    Resolution;   

DOI  :  10.1016/0014-5793(94)80122-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Pertussis toxin, both complete and the B-oligomer, were imaged by atomic force miroscopy (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°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.

【 授权许可】

Unknown