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  The c13 Ring from a Thermoalkaliphilic ATP Synthase Reveals an Extended Diameter Due to a Special Structural Region

Matthies, D., Preiss, L., Klyszejko, A. L., Muller, D. J., Cook, G. M., Vonck, J., et al. (2009). The c13 Ring from a Thermoalkaliphilic ATP Synthase Reveals an Extended Diameter Due to a Special Structural Region. Journal of Molecular Biology, 388(3), 611-618. doi:10.1016/j.jmb.2009.03.052.

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 Creators:
Matthies, Doreen1, Author           
Preiss, Laura1, Author           
Klyszejko, Adriana L.2, Author
Muller, Daniel J.2, Author
Cook, Gregory M.3, Author
Vonck, Janet1, Author           
Meier, Thomas1, 4, Author           
Affiliations:
1Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068291              
2Biotechnology Center, University of Technology Dresden, 01307 Dresden, Germany, ou_persistent22              
3Department of Microbiology and Immunology, Otago School of Medical Sciences, University of Otago, Dunedin, New Zealand, ou_persistent22              
4Cluster of Excellence Macromolecular Complexes, Max Planck Institute of Biophysics, 60438 Frankfurt am Main, Germany, ou_persistent22              

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Free keywords: F1Fo-ATP synthase c-ring; thermoalkaliphilic Bacillus sp. strain TA2.A1; electron microscopy; atomic force microscopy; 2D crystallization
 Abstract: We have structurally characterized the c-ring from the thermoalkaliphilic Bacillus sp. strain TA2.A1 F1Fo-ATP synthase. Atomic force microscopy imaging and cryo-electron microscopy analyses confirm previous mass spectrometric data indicating that this c-ring contains 13 c-subunits. The cryo-electron microscopy map obtained from two-dimensional crystals shows less closely packed helices in the inner ring compared to those of Na+-binding c11 rings. The inner ring of α-helices in c11 rings harbors a conserved GxGxGxGxG motif, with glycines located at the interface between c-subunits, which is responsible for the close packing of these helices. This glycine motif is altered in the c13 ring of Bacillus sp. strain TA2.A1 to AxGxSxGxS, leading to a change in c–c subunit contacts and thereby enlarging the c-ring diameter to host a greater number of c-subunits. An altered glycine motif is a typical feature of c-subunit sequences in alkaliphilic Bacillus species. We propose that enlarged c-rings in proton-dependent F-ATP synthases may represent an adaptation to facilitate ATP synthesis at low overall proton-motive force, as occurs in bacteria that grow at alkaline pH.

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Language(s): eng - English
 Dates: 2009-03-182009-02-042009-03-192009-03-242009-05-08
 Publication Status: Published in print
 Pages: 8
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/j.jmb.2009.03.052
PMID: 19327366
 Degree: -

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Title: Journal of Molecular Biology
  Other : JMB
  Abbreviation : J. Mol. Biol.
Source Genre: Journal
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Affiliations:
Publ. Info: Elsevier
Pages: - Volume / Issue: 388 (3) Sequence Number: - Start / End Page: 611 - 618 Identifier: ISSN: 0022-2836
CoNE: https://pure.mpg.de/cone/journals/resource/0022-2836