| Enhanced internal ionic interaction of MFS efflux pump MdfA contributes to its elevated antibiotic export. | Enhanced internal ionic interaction of MFS efflux pump MdfA contributes to its elevated antibiotic export.
Li Y, Ge X. | 12/31/2022 |
| Probing the solution structure of the E. coli multidrug transporter MdfA using DEER distance measurements with nitroxide and Gd(III) spin labels. | Probing the solution structure of the E. coli multidrug transporter MdfA using DEER distance measurements with nitroxide and Gd(III) spin labels.
Yardeni EH, Bahrenberg T, Stein RA, Mishra S, Zomot E, Graham B, Tuck KL, Huber T, Bibi E, Mchaourab HS, Goldfarb D., Free PMC Article | 11/21/2020 |
| analysis of MdfA variant I239T/G354E in complexes with three electrically different ligands reveals the molecular basis for substrate recognition | Structure of an engineered multidrug transporter MdfA reveals the molecular basis for substrate recognition.
Wu HH, Symersky J, Lu M., Free PMC Article | 05/2/2020 |
| Outward open conformation of the Major Facilitator Superfamily multidrug/H(+) antiporter MdfA from Escherichia coli has changes in relative orientations of the N- and C-terminal lobes, and transmembrane helix5 (TM5) is kinked and twisted. In vitro reconstitution experiments demonstrate the importance of selected residues for transport and molecular dynamics simulations provide insights into antiporter switching. | Outward open conformation of a Major Facilitator Superfamily multidrug/H(+) antiporter provides insights into switching mechanism.
Nagarathinam K, Nakada-Nakura Y, Parthier C, Terada T, Juge N, Jaenecke F, Liu K, Hotta Y, Miyaji T, Omote H, Iwata S, Nomura N, Stubbs MT, Tanabe M., Free PMC Article | 01/12/2019 |
| MdfA has exceptional promiscuous capabilities not only in its interaction with a plethora of chemically dissimilar compounds, but also concerning the various faces of its modes of energy consumption. [review] | The fascinating but mysterious mechanistic aspects of multidrug transport by MdfA from Escherichia coli.
Yardeni EH, Zomot E, Bibi E. | 11/10/2018 |
| Crystallization and X-ray diffraction analysis of the multidrug-resistance transporter MdfA from Escherichia coli has been reported. | The multidrug-resistance transporter MdfA from Escherichia coli: crystallization and X-ray diffraction analysis.
Nagarathinam K, Jaenecke F, Nakada-Nakura Y, Hotta Y, Liu K, Iwata S, Stubbs MT, Nomura N, Tanabe M., Free PMC Article | 12/9/2017 |
| The MdfA structure consists of four pseudo-symmetrical, three-helix repeats, consistent with the typical structure of an MFS transporter. | Substrate-bound structure of the E. coli multidrug resistance transporter MdfA.
Heng J, Zhao Y, Liu M, Liu Y, Fan J, Wang X, Zhao Y, Zhang XC., Free PMC Article | 06/11/2016 |
| The mdfA gene can function as transporter responsible for multidrug resistance, and also mediated the synergistic function with its surrounding genes in conjugative plasmids. | Structural and environmental features of novel mdfA variant and mdfA genes in recombinant regions of Escherichia coli.
Wang D, Liang H, Chen J, Mou Y, Qi Y. | 05/30/2015 |
| GlpG is able to recognize and cleave truncated forms of MdfA but not the intact protein. | Cleavage of a multispanning membrane protein by an intramembrane serine protease.
Erez E, Bibi E. | 01/21/2010 |
| the Mdr-binding pocket of MdfA is conformationally sensitive | A promiscuous conformational switch in the secondary multidrug transporter MdfA.
Fluman N, Cohen-Karni D, Weiss T, Bibi E., Free PMC Article | 01/21/2010 |
| results suggest that in the absence of specific chloramphenicol selection pressure, the cmlA gene is maintained by virtue of gene linkage to genes encoding resistance to antimicrobials that are currently approved for use in food animals | The chloramphenicol resistance gene cmlA is disseminated on transferable plasmids that confer multiple-drug resistance in swine Escherichia coli.
Bischoff KM, White DG, Hume ME, Poole TL, Nisbet DJ. | 01/21/2010 |
| Arg112 is important for multidrug transport by MdfA. | 3D model of the Escherichia coli multidrug transporter MdfA reveals an essential membrane-embedded positive charge.
Sigal N, Vardy E, Molshanski-Mor S, Eitan A, Pilpel Y, Schuldiner S, Bibi E. | 01/21/2010 |
| results show that MdfA confers extreme alkaline pH resistance and allows the growth of transformed cells under conditions that are close to those used normally by alkaliphiles (up to pH 10) by maintaining a physiological internal pH | Alkalitolerance: a biological function for a multidrug transporter in pH homeostasis.
Lewinson O, Padan E, Bibi E., Free PMC Article | 01/21/2010 |
| properties of MdfA including its multidrug recognition capacity, proton recognition determinants, aspects of energy utilization, and physiological role [review] | MdfA from Escherichia coli, a model protein for studying secondary multidrug transport.
Sigal N, Cohen-Karni D, Siemion S, Bibi E. | 01/21/2010 |
| In this study, we got an evidence that MdfA is a chloramphenicol/H+ antiporter. | Evidence for chloramphenicol/H+ antiport in Cmr (MdfA) system of Escherichia coli and properties of the antiporter.
Mine T, Morita Y, Kataoka A, Mizushima T, Tsuchiya T. | 02/16/2006 |