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.
Original language | English |
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Pages (from-to) | 3898-3907 |
Number of pages | 10 |
Journal | FEBS Letters |
Volume | 594 |
Issue number | 23 |
Early online date | 18-Aug-2020 |
DOIs | |
Publication status | Published - Dec-2020 |
Keywords
- ABC transporter
- antibiotics uptake
- Mycobacterium tuberculosis
- non-specific uptake
- transport mechanism
- ESCHERICHIA-COLI SBMA
- GENETIC-ANALYSIS
- ANTIMICROBIAL PEPTIDES
- ABC TRANSPORTER
- BACA PROTEIN
- IDENTIFICATION
- BINDING
- RESISTANCE
- MUTATIONS
- SEQUENCE