期刊
FEBS LETTERS
卷 594, 期 23, 页码 3898-3907出版社
WILEY
DOI: 10.1002/1873-3468.13912
关键词
ABC transporter; antibiotics uptake; Mycobacterium tuberculosis; non-specific uptake; transport mechanism
资金
- Dutch Research Council (NWO)
- National Institutes of Health [R01-GM129325]
- Office of Cyber Infrastructure and Computational Biology, National Institute of Allergy and Infectious Diseases
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 fromMycobacterium tuberculosishas 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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