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

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.

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 Creators:
Meier, Thomas, Author
Ferguson, Scott A., Author
Cook, Gregory M., Author
Dimroth, Peter, Author
Vonck, Janet1, Author                 
Affiliations:
1Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068291              

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Free keywords: Membrane proteins; Clostridium paradoxum
 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.

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Language(s): eng - English
 Dates: 2006-11
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 305045
DOI: 10.1128/JB.00934-06
 Degree: -

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Title: Journal of Bacteriology
  Other : J. Bacteriol.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Washington, DC : American Society for Microbiology (ASM)
Pages: - Volume / Issue: 188 Sequence Number: - Start / End Page: 7759 - 7764 Identifier: ISSN: 0021-9193
CoNE: https://pure.mpg.de/cone/journals/resource/954925410823