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Bacterial multi‐solute transporters
Author(s) -
Slotboom Dirk J.,
Ettema Thijs W.,
Nijland Mark,
Thangaratnarajah Chancievan
Publication year - 2020
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13912
Subject(s) - atp binding cassette transporter , transporter , nucleotide , biology , transport protein , protein family , membrane transport protein , antibiotics , solute carrier family , biochemistry , chemistry , computational biology , gene
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.