A cryoelectron microscopy study of the interaction of the Escherichia coli F 1 -ATPase with subunit b dimer

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Abstract

A complex between the Escherichia coli F 1 -ATPase and a truncated form of the ECF 0 -b subunit was formed and examined by cryoelectron microscopy in amorphous ice. Image analysis of single particles in the hexagonal projection revealed that the polar domain of the b subunit interacts with a β subunit different from the one which interacts with the ε{lunate} subunit. The cavity in the enzyme, visible in the hexagonal projection, is not filled by the b polypeptide, therefore leaving enough room for extensive conformational changes of the γ and ε{lunate} subunits within the native F 1 F 0 complex. © 1994.

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Wilkens, S., Dunn, S. D., & Capaldi, R. A. (1994). A cryoelectron microscopy study of the interaction of the Escherichia coli F 1 -ATPase with subunit b dimer. FEBS Letters, 354(1), 37–40. https://doi.org/10.1016/0014-5793(94)01059-5

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