| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 2052562 | FEBS Letters | 2005 | 4 Pages |
Abstract
The osmotically regulated OpuA uptake system from Bacillus subtilis is a member of the SBP-dependent subfamily of ABC-transporters. The functional complex, OpuA(A2B2C), catalyzes the osmotically controlled import of the compatible solutes glycine betaine and proline betaine. Here, we describe the purification of the isolated TMS, OpuAB. Stimulated ATPase activity of OpuAA by OpuAB demonstrated that OpuAB adopts a functional fold. An interaction between all subunits could be verified in detergent solution with the highest ATPase stimulation determined for the dimeric NBS in the re-associated complex in the presence of all transport components plus substrate.
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Authors
Carsten Horn, Erhard Bremer, Lutz Schmitt,