Bacterial multi‐solute transporters. Issue 23 (10th September 2020)

• Record Type: Journal Article
• Authors: Slotboom, Dirk J.; Ettema, Thijs W.; Nijland, Mark; Thangaratnarajah, Chancievan
• Is Part Of: FEBS letters. Volume 594:Issue 23(2020)
• Page Start: 3898
• Page End: 3907
• Publication Date: 2020-09-10
• Subjects: ABC transporter -- antibiotics uptake -- Mycobacterium tuberculosis -- non‐specific uptake -- transport mechanism; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1002/1873-3468.13912
• Languages: English
• ISSNs: 0014-5793

Abstract

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.