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

FEBS Letters

Iwamoto-Kihara, Atsuko¹  Futai, Masamitsu¹  Nettikadan, Saju²  Tokumasu, Fuyuki²  Omote, Hiroshi¹  Takeyasu, Kunio² 

[1]Division of Biological Science, The Institute of Scientific and Industrial Research, Osaka University, Ibaraki, Osaka 567, Japan

[2]Department of Medical Biochemistry, and Neurobiotechnology Center, The Ohio State University, Columbus, OH 43210, USA

关键词: AFM;    F0F1-ATPase;    ATP synthase;    H+-channel;    Subunit assembly;   

DOI  :  10.1016/0014-5793(96)00796-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The structure of Escherichia coli F₀F₁-ATPase (ATP synthase), and its F₀ 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 , and a height of from the membrane surface. F₀ sectors were visualized as two different ring-like structures (one with a central mass and the other with a central hollow of depth) with a calculated outer diameter of . 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 subunits in the F₀ sector. Considering the stoichiometry of F₀ subunits, the area of the image observed is large enough to accommodate all three F₀ subunits in an asymmetric manner.

【 授权许可】

Unknown