Abstract
The RND efflux pump AcrAB-TolC is involved in antibiotic resistance in E. coli [1-2]. The core of this machinery is the proton-gradient-driven antiporter AcrB, a homotrimeric protein with an unreached ability to recognize antibiotics belonging to many different families. On the basis of available experimental data, a functional rotation mechanism has been hypothesized for this transporter, in which recognition and expulsion of substrates are coupled to concerted conformational changes occurring in each monomer of AcrB.
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