STRUCTURE AND STABILITY OF PERTUSSIS TOXIN STUDIED BY IN-SITU ATOMIC-FORCE MICROSCOPY

被引：71
|
作者：
YANG, J
MOU, JX
SHAO, ZF
机构：
[1] UNIV VIRGINIA, DEPT MOLEC PHYSIOL & BIOL, BIO SPM LAB, CHARLOTTESVILLE, VA 22908 USA
[2] UNIV VIRGINIA, BIOPHYS PROGRAM, CHARLOTTESVILLE, VA 22908 USA
来源：
FEBS LETTERS | 1994年 / 338卷 / 01期
关键词：
ATOMIC FORCE MICROSCOPY; PERTUSSIS TOXIN; STRUCTURE; RESOLUTION;
D O I：
10.1016/0014-5793(94)80122-3
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
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 degrees 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.
引用
收藏
页码：89 / 92
页数：4
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