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• W2950197647 abstract "Abstract MdfA is a prototypical H + -coupled multidrug transporter that is characterized by extraordinarily broad substrate specificity. The involvement of specific H-bonds in MdfA-drug interactions and the simplicity of altering the substrate specificity of MdfA contradict the promiscuous nature of multidrug recognition, presenting a baffling conundrum. Here we show the X-ray structures of MdfA variant I239T/G354E in complexes with three electrically different ligands, determined at resolutions up to 2.2 Å. Our structures reveal that I239T/G354E interacts with these compounds differently from MdfA and that I239T/G354E possesses two discrete, non-overlapping substrate-binding sites. Our results shed new light on the molecular design of multidrug-binding and protonation sites and highlight the importance of often-neglected, long-range charge-charge interactions in multidrug recognition. Beyond helping to solve the ostensible conundrum of multidrug recognition, our findings suggest the mechanistic difference between substrate and inhibitor for any H + -dependent multidrug transporter, which may open new vistas on curtailing efflux-mediated multidrug resistance." @default.
• W2950197647 created "2019-06-27" @default.
• W2950197647 creator A5024180387 @default.
• W2950197647 creator A5029818680 @default.
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• W2950197647 date "2019-06-17" @default.
• W2950197647 modified "2023-09-25" @default.
• W2950197647 title "Structure of an engineered multidrug transporter MdfA reveals the molecular basis for substrate recognition" @default.
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• W2950197647 doi "https://doi.org/10.1038/s42003-019-0446-y" @default.
• W2950197647 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6572762" @default.
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• W2950197647 hasPublicationYear "2019" @default.
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