ArticleThe Journal of biological chemistry2009
A promiscuous conformational switch in the secondary multidrug transporter MdfA.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Mutagenesis and functional analysis of SotB: A multidrug transporter of the major facilitator superfamily fromFrontiers in microbiology · 2022Article
- Structures and General Transport Mechanisms by the Major Facilitator Superfamily (MFS).Chemical reviews · 2021Article
- Probing the solution structure of the E. coli multidrug transporter MdfA using DEER distance measurements with nitroxide and Gd(III) spin labels.Scientific reports · 2019Article
- smFRET Probing Reveals Substrate-Dependent Conformational Dynamics of E. coli Multidrug MdfA.Biophysical journal · 2019Article
- Structure of an engineered multidrug transporter MdfA reveals the molecular basis for substrate recognition.Communications biology · 2019Article
- Outward open conformation of a Major Facilitator Superfamily multidrug/HNature communications · 2018Article
- The multidrug-resistance transporter MdfA from Escherichia coli: crystallization and X-ray diffraction analysis.Acta crystallographica. Section F, Structural biology communications · 2017Article
- Insight into determinants of substrate binding and transport in a multidrug efflux protein.Scientific reports · 2016Article
- Recent advances toward a molecular mechanism of efflux pump inhibition.Frontiers in microbiology · 2015Review
- Dissection of mechanistic principles of a secondary multidrug efflux protein.Molecular cell · 2012Article
- Manipulating the drug/proton antiport stoichiometry of the secondary multidrug transporter MdfA.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Structural comparison of bacterial multidrug efflux pumps of the major facilitator superfamily.Trends in cell & molecular biologyArticle
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4 authors.
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Abstract
Multidrug (Mdr) transporters are membrane proteins that actively export structurally dissimilar drugs from the cell, thereby rendering the cell resistant to toxic compounds. Similar to substrate-specific transporters, Mdr transporters also undergo substrate-induced conformational changes. However, the mechanism by which a variety of dissimilar substrates are able to induce similar transport-compatible conformational responses in a single transporter remains unclear. To address this major aspect of Mdr transport, we studied the conformational behavior of the Escherichia coli Mdr transporter MdfA. Our results show that indeed, different substrates induce similar conformational changes in the transporter. Intriguingly, in addition, we observed that compounds other than substrates are able to confer similar conformational changes when covalently attached at the putative Mdr recognition pocket of MdfA. Taken together, the results suggest that the Mdr-binding pocket of MdfA is conformationally sensitive. We speculate that the same conformational switch that usually drives active transport is triggered promiscuously by merely occupying the Mdr-binding site.
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