A novel packing arrangement of AcrB in the lipid bilayer membrane. Issue 24 (15th November 2014)

• Record Type: Journal Article
• Authors: Ly, K.; Bartho, J.D.; Eicher, T.; Pos, K.M.; Mitra, A.K.
• Is Part Of: FEBS letters. Volume 588:Issue 24(2014)
• Page Start: 4776
• Page End: 4783
• Publication Date: 2014-11-15
• Subjects: AcrB -- Multi-drug efflux -- 2-D crystal -- Electron crystallography; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1016/j.febslet.2014.11.010
• Languages: English
• ISSNs: 0014-5793

Abstract

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. Abstract : E. coli lipid reconstituted AcrB 2D crystals show predominantly asymmetric trimers. Inter monomer–monomer interactions stabilize adjacent AcrB trimers in 2D crystal. Crystals of AcrB containing non‐trimeric arrangement of monomers were also observed.