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J Mol Biol. 2009 May 8;388(3):611-8. doi: 10.1016/j.jmb.2009.03.052. Epub 2009 Mar 24.

The c13 ring from a thermoalkaliphilic ATP synthase reveals an extended diameter due to a special structural region.

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Max Planck Institute of Biophysics, Max-von-Laue-Strasse 3, Frankfurt am Main, Germany.


We have structurally characterized the c-ring from the thermoalkaliphilic Bacillus sp. strain TA2.A1 F(1)F(o)-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 c(11) rings. The inner ring of alpha-helices in c(11) 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 c(13) 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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