AI Article Synopsis
- Bacterial membrane proteins from the SbmA/BacA family are involved in transporting various hydrophilic molecules, including antibiotics and antimicrobial peptides.
- These proteins can be full-length ATP-binding cassette (ABC) transporters or truncated versions that operate without ATP.
- Recent cryo-EM studies of Rv1819c from Mycobacterium tuberculosis have revealed insights into how these transporters work, raising questions about how their design leads to the unintended import of antibiotics and what physiological processes they might support.
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.
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| http://dx.doi.org/10.1002/1873-3468.13912 | DOI Listing |
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