| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10870044 | FEBS Letters | 2014 | 8 Pages |
Abstract
The central component AcrB of the Escherichia coli drug efflux complex AcrA-AcrB-TolC has been extensively investigated by X-ray crystallography of detergent-protein 3-D crystals. In these crystals, AcrB packs as trimers - the functional unit. We visualized the AcrB-AcrB interaction in its native environment by examining E. coli lipid reconstituted 2-D crystals, which were overwhelmingly formed by asymmetric trimers stabilized by strongly-interacting monomers from adjacent trimers. Most interestingly, we observed lattices formed by an arrangement of AcrB monomers distinct from that in traditional trimers. This hitherto unobserved packing, might play a role in the biogenesis of trimeric AcrB.
Keywords
Related Topics
Life Sciences
Agricultural and Biological Sciences
Plant Science
Authors
K. Ly, J.D. Bartho, T. Eicher, K.M. Pos, A.K. Mitra,