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Journal of Bacteriology, November 2006, p. 7759-7764, Vol. 188, No. 22
0021-9193/06/$08.00+0     doi:10.1128/JB.00934-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

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

Institut für Mikrobiologie, ETH Zürich, Wolfgang-Pauli-Str. 10, CH-8093 Zürich, Switzerland,¹ Department of Microbiology and Immunology, Otago School of Medical Sciences, University of Otago, P.O. Box 56, Dunedin, New Zealand,² Max-Planck-Institute of Biophysics, Max-von-Laue-Str. 3, D-60438 Frankfurt, Germany³

Received 28 June 2006/ Accepted 5 September 2006

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 Å resolution. In the projection map, each c ring consists of two concentric, slightly staggered, packed rings, each composed of 11 densities representing the -helices. On the basis of these results, it was determined that the F-ATPase from C. paradoxum contains an undecameric c ring.

Published ahead of print on 15 September 2006.

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