This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Meier, T.
Right arrow Articles by Vonck, J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Meier, T.
Right arrow Articles by Vonck, J.

 Previous Article  |  Next Article 

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{triangledown}

Thomas Meier,1* Scott A. Ferguson,2 Gregory M. Cook,2 Peter Dimroth,1 and Janet Vonck3

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 {alpha}-helices. On the basis of these results, it was determined that the F-ATPase from C. paradoxum contains an undecameric c ring.

* Corresponding author. Mailing address: Max-Planck-Institute of Biophysics, Max-von-Laue-Str. 3, D-60438 Frankfurt, Germany. Phone: 49-69-63033038. Fax: 49-69-63033002. E-mail: thomas.meier{at}mpibp-frankfurt.mpg.de.

{triangledown} Published ahead of print on 15 September 2006.

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.



This article has been cited by other articles:

  • Vollmar, M., Schlieper, D., Winn, M., Buchner, C., Groth, G. (2009). Structure of the c14 Rotor Ring of the Proton Translocating Chloroplast ATP Synthase. J. Biol. Chem. 284: 18228-18235 [Abstract] [Full Text]  
  • Vonck, J., Pisa, K. Y., Morgner, N., Brutschy, B., Muller, V. (2009). Three-dimensional Structure of A1A0 ATP Synthase from the Hyperthermophilic Archaeon Pyrococcus furiosus by Electron Microscopy. J. Biol. Chem. 284: 10110-10119 [Abstract] [Full Text]  
  • Ballhausen, B., Altendorf, K., Deckers-Hebestreit, G. (2009). Constant c10 Ring Stoichiometry in the Escherichia coli ATP Synthase Analyzed by Cross-Linking. J. Bacteriol. 191: 2400-2404 [Abstract] [Full Text]  
  • Pogoryelov, D., Reichen, C., Klyszejko, A. L., Brunisholz, R., Muller, D. J., Dimroth, P., Meier, T. (2007). The Oligomeric State of c Rings from Cyanobacterial F-ATP Synthases Varies from 13 to 15. J. Bacteriol. 189: 5895-5902 [Abstract] [Full Text]  
  • McMillan, D. G. G., Keis, S., Dimroth, P., Cook, G. M. (2007). A Specific Adaptation in the a Subunit of Thermoalkaliphilic F1FO-ATP Synthase Enables ATP Synthesis at High pH but Not at Neutral pH Values. J. Biol. Chem. 282: 17395-17404 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»