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Substrate-bound structure of the E. coli multidrug resistance transporter MdfA


Multidrug resistance is a serious threat to public health. Proton motive force-driven antiporters from the major facilitator superfamily (MFS) constitute a major group of multidrug-resistance transporters. Currently, no reports on crystal structures of MFS antiporters in complex with their substrates exist. The E. coli MdfA transporter is a well-studied model system for biochemical analyses of multidrug-resistance MFS antiporters. Here, we report three crystal structures of MdfA-ligand complexes at resolutions up to 2.0 angstrom, all in the inward-facing conformation. The substrate-binding site sits proximal to the conserved acidic residue, D34. Our mutagenesis studies support the structural observations of the substrate-binding mode and the notion that D34 responds to substrate binding by adjusting its protonation status. Taken together, our data unveil the substrate-binding mode of MFS antiporters and suggest a mechanism of transport via this group of transporters.
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Recommended references: Heng, Jie,Zhao, Yan,Liu, Yue,Fan, Junping,Wang, Xianping,Zhao, Yongfang,Zhang, Xuejun C.,Heng, Jie,Zhao, Yan,Liu, Ming.(2016).Substrate-bound structure of the E. coli multidrug resistance transporter MdfA.CELL RESEARCH.[ChinaXiv:201605.01368] (Click&Copy)
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[V1] 2016-05-12 08:40:38 chinaXiv:201605.01368V1 Download
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