Abstract:
:Secondary multidrug transporters use ion concentration gradients to energize the removal from cells of various antibiotics. The Escherichia coli multidrug transporter MdfA exchanges a single proton with a single monovalent cationic drug molecule. This stoichiometry renders the efflux of divalent cationic drugs energetically unfavourable, as it requires exchange with at least two protons. Here we show that surprisingly, MdfA catalyses efflux of divalent cations, provided that they have a unique architecture: the two charged moieties must be separated by a long linker. These drugs are exchanged for two protons despite the apparent inability of MdfA to exchange two protons for a single drug molecule. Our results suggest that these drugs are transported in two consecutive transport cycles, where each cationic moiety is transported as if it were a separate substrate. We propose that secondary transport can adopt a processive-like mode of action, thus expanding the substrate spectrum of multidrug transporters.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Fluman N,Adler J,Rotenberg SA,Brown MH,Bibi Edoi
10.1038/ncomms5615subject
Has Abstractpub_date
2014-08-08 00:00:00pages
4615issn
2041-1723pii
ncomms5615journal_volume
5pub_type
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