Bacterial multi-solute transporters

D J Slotboom; T W Ettema; M Nijland; C Thangaratnarajah

doi:10.1002/1873-3468.13912

Bacterial multi-solute transporters

D J Slotboom^*, T W Ettema, M Nijland, C Thangaratnarajah

^*Corresponding author for this work

Enzymology

Research output: Contribution to journal › Review article › peer-review

12 Citations (Scopus)

104 Downloads (Pure)

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
Pages (from-to)	3898-3907
Number of pages	10
Journal	FEBS Letters
Volume	594
Issue number	23
Early online date	18-Aug-2020
DOIs	https://doi.org/10.1002/1873-3468.13912
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

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10.1002/1873-3468.13912Licence: CC BY-NC

Bacterial multi‐solute transportersFinal publisher's version, 5.88 MBLicence: CC BY-NC

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oLife Fellowship Programme
Roos, W. (PI), van der Tak, F. (PI), Zijlstra, W. (PI), Dobos, V. (Postdoc), Heinen, L. (Postdoc), Thangaratnarajah, C. (Postdoc), Hoekzema, M. (Postdoc), Blokhuis, A. (Postdoc), Mascotti, L. (Postdoc), Padin Santos, D. (Postdoc), Chopra, A. (Postdoc), Obermaier, S. (Postdoc), Driver, M. (Postdoc), Moreira Goulart, M. (Postdoc), Sasidharan, S. (Postdoc), Samar Mahapatra, S. (Postdoc), Zylstra, A. (Postdoc), Geiger, Y. (Postdoc), Llopis Lorente, A. (Postdoc), Aschmann, D. (Postdoc) & Kulala Vittala, S. (Postdoc)
01/04/2019 → 31/03/2024
Project: Research

Cite this

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title = "Bacterial multi-solute transporters",

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.",

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",

author = "Slotboom, {D J} and Ettema, {T W} and M Nijland and C Thangaratnarajah",

year = "2020",

month = dec,

doi = "10.1002/1873-3468.13912",

language = "English",

volume = "594",

pages = "3898--3907",

journal = "FEBS Letters",

issn = "0014-5793",

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TY - JOUR

T1 - Bacterial multi-solute transporters

AU - Slotboom, D J

AU - Ettema, T W

AU - Nijland, M

AU - Thangaratnarajah, C

PY - 2020/12

Y1 - 2020/12

N2 - 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.

AB - 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.

KW - ABC transporter

KW - antibiotics uptake

KW - Mycobacterium tuberculosis

KW - non-specific uptake

KW - transport mechanism

KW - ESCHERICHIA-COLI SBMA

KW - GENETIC-ANALYSIS

KW - ANTIMICROBIAL PEPTIDES

KW - ABC TRANSPORTER

KW - BACA PROTEIN

KW - IDENTIFICATION

KW - BINDING

KW - RESISTANCE

KW - MUTATIONS

KW - SEQUENCE

U2 - 10.1002/1873-3468.13912

DO - 10.1002/1873-3468.13912

M3 - Review article

C2 - 32810294

SN - 0014-5793

VL - 594

SP - 3898

EP - 3907

JO - FEBS Letters

JF - FEBS Letters

IS - 23

ER -

Bacterial multi-solute transporters

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Keywords

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