The bacterial ABC transporter BmrA
The family of ATP-binding cassette (ABC) transporters is one of the biggest known protein familiy. Family members can be found in prokaryotes as well as in eukaryotes. The transporters are integral membrane proteins, consisting of transmembrane and nucleotide-binding domains. With the energy of ATP-hydrolysis, substrates are transported across biomembranes, and the substrates can involve e.g. anti-cancer drugs used as therapeutics, which then contacts a chemo-therapy.
Modulating the activity of ABC transporters by small molecules could thus support certain therapies and could be used to treat various diseases.
Our current research focusses on the ABC-transporter BmrA, an ABC transporter from the bacterium Bacillus subtilis that shows a high sequence homology to human and other bacterial ABC transporters. Our analysis of this bacterial protein allows in-deep biochemical and biophysical analyses that will enable us to better understand the molecular details of ABC-transporter activities. This certainly is the basis for the next step: identifying ABC-transporter modulators.
Read more:
- Osten, V., Nitzpon, D. L., Baier, A., Moeller, A. and Schneider, D. (2026). A Salt Bridge Pre-arranges the Structure of the ABC Transporter BmrA for Proper NBD Dimerization, J. Mol. Biol., 438 (13), 169794. https://doi.org/10.1016/j.jmb.2026.169794
- Osten, V. and Schneider, D. (2025). Membrane properties control the ATPase activity of the ABC transporter BmrA. Biochim. Biophys. Acta – Biomembranes, 1867, 184430. https://doi.org/10.1016/j.bbamem.2025.184430