Molecular imaging of Escherichia coli F0F1-ATPase in reconstituted membranes using atomic force microscopy

被引:109
作者
Takeyasu, K
Omote, H
Nettikadan, S
Tokumasu, F
IwamotoKihara, A
Futai, M
机构
[1] OHIO STATE UNIV,NEUROBIOTECHNOL CTR,COLUMBUS,OH 43210
[2] KYOTO UNIV,FAC INTEGRATED HUMAN STUDIES,DEPT NAT ENVIRONM SCI,KYOTO 60601,JAPAN
[3] OSAKA UNIV,INST SCI & IND RES,DIV BIOL SCI,IBARAKI,OSAKA 567,JAPAN
关键词
AFM; F0F1-ATPase; ATP synthase; H+-channel; subunit assembly;
D O I
10.1016/0014-5793(96)00796-X
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
The structure of Escherichia coli F0F1-ATPase (ATP synthase), and its F-0 sector reconstituted in lipid membranes was analyzed using atomic force microscopy (AFM) by tapping-mode operation, The majority of F0F1-ATPases were visualized as spheres with a calculated diameter of similar to 90 Angstrom, and a height of similar to 100 Angstrom from the membrane surface. F-o sectors were visualized as two different ring-like structures (one with a central mass and the other with a central hollow of greater than or equal to 18 Angstrom depth) with a calculated outer diameter of similar to 130 Angstrom. The two different images possibly represent the opposite orientations of the complex in the membranes. The ring-like projections of both images suggest inherently asymmetric assemblies of the submits in the F-0 sector, Considering the stoichiometry of F-0 submits, the area of the image observed is large enough to accommodate all three F-0 subunits in an asymmetric manner.
引用
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页码:110 / 113
页数:4
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