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Journal Article

Structural Investigations of the Membrane-Embedded Rotor Ring of F-ATPase from Clostridium paradoxum

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Vonck,  Janet       
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Meier, T., Ferguson, S. A., Cook, G. M., Dimroth, P., & Vonck, J. (2006). Structural Investigations of the Membrane-Embedded Rotor Ring of F-ATPase from Clostridium paradoxum. Journal of Bacteriology, 188, 7759-7764. doi:10.1128/JB.00934-06.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0024-D951-0
Abstract
The Na(+)-translocating F-ATPase of the thermoalkaliphilic bacterium Clostridium paradoxum harbors an oligomeric ring of c subunits that resists dissociation by sodium dodecyl sulfate. The c ring has been isolated and crystallized in two dimensions. From electron microscopy of these c-ring crystals, a projection map was calculated to 7 A resolution. In the projection map, each c ring consists of two concentric, slightly staggered, packed rings, each composed of 11 densities representing the alpha-helices. On the basis of these results, it was determined that the F-ATPase from C. paradoxum contains an undecameric c ring.