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. 2020 Dec;594(23):3898-3907.
doi: 10.1002/1873-3468.13912. Epub 2020 Sep 10.

Bacterial multi-solute transporters

Dirk J Slotboom  1 , Thijs W Ettema  1 , Mark Nijland  1 , Chancievan Thangaratnarajah  1
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Free article

Bacterial multi-solute transporters

Dirk J Slotboom et al. FEBS Lett. 2020 Dec.
Free article

Abstract

Bacterial membrane proteins of the SbmA/BacA family are multi-solute transporters that mediate the uptake of structurally diverse hydrophilic molecules, including aminoglycoside antibiotics and antimicrobial peptides. Some family members are full-length ATP-binding cassette (ABC) transporters, whereas other members are truncated homologues that lack the nucleotide-binding domains and thus mediate ATP-independent transport. A recent cryo-EM structure of the ABC transporter Rv1819c from Mycobacterium tuberculosis has shed light on the structural basis for multi-solute transport and has provided insight into the mechanism of transport. Here, we discuss how the protein architecture makes SbmA/BacA family transporters prone to inadvertent import of antibiotics and speculate on the question which physiological processes may benefit from multi-solute transport.

Keywords: Mycobacterium tuberculosis; ABC transporter; antibiotics uptake; non-specific uptake; transport mechanism.

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