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- W2769367061 abstract "Antibiotic efflux is one of the most critical mechanisms leading to bacterial multidrug resistance. Antibiotics are effluxed out of the bacterial cell by a tripartite efflux pump, a complex machinery comprised of outer membrane, periplasmic adaptor, and inner membrane protein components. Understanding the mechanism of efflux pump assembly and its dynamics could facilitate discovery of novel approaches to counteract antibiotic resistance in bacteria. We built here an intact atomistic model of the Pseudomonas aeruginosa MexAB-OprM pump in a Gram-negative membrane model that contained both inner and outer membranes separated by a periplasmic space. All-atom molecular dynamics (MD) simulations confirm that the fully assembled pump is stable in the microsecond timescale. Using a combination of all-atom and coarse-grained MD simulations and sequence covariation analysis, we characterized the interface between MexA and OprM in the context of the entire efflux pump. These analyses suggest a plausible mechanism by which OprM is activated via opening of its periplasmic aperture through a concerted interaction with MexA." @default.
- W2769367061 created "2017-12-04" @default.
- W2769367061 creator A5001257836 @default.
- W2769367061 creator A5063460625 @default.
- W2769367061 creator A5070008549 @default.
- W2769367061 creator A5082022500 @default.
- W2769367061 creator A5087340766 @default.
- W2769367061 date "2017-11-28" @default.
- W2769367061 modified "2023-10-02" @default.
- W2769367061 title "Dynamics of Intact MexAB-OprM Efflux Pump: Focusing on the MexA-OprM Interface" @default.
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