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Crystal structure of AcrB in complex with a single transmembrane subunit reveals another twist

Törnroth-Horsefield, Susanna LU ; Gourdon, Pontus LU ; Horsefield, Rob ; Brive, Lars ; Yamamoto, Natsuko ; Mori, Hirotada ; Snijder, Arjan and Neutze, Richard (2007) In Structure 15(12). p.73-1663
Abstract

Bacterial drug resistance is a serious concern for human health. Multidrug efflux pumps export a broad variety of substrates out of the cell and thereby convey resistance to the host. In Escherichia coli, the AcrB:AcrA:TolC efflux complex forms a principal transporter for which structures of the individual component proteins have been determined in isolation. Here, we present the X-ray structure of AcrB in complex with a single transmembrane protein, assigned by mass spectrometry as YajC. A specific rotation of the periplasmic porter domain of AcrB is also revealed, consistent with the hypothesized "twist-to-open" mechanism for TolC activation. Growth experiments with yajc-deleted E. coli reveal a modest increase in the organism's... (More)

Bacterial drug resistance is a serious concern for human health. Multidrug efflux pumps export a broad variety of substrates out of the cell and thereby convey resistance to the host. In Escherichia coli, the AcrB:AcrA:TolC efflux complex forms a principal transporter for which structures of the individual component proteins have been determined in isolation. Here, we present the X-ray structure of AcrB in complex with a single transmembrane protein, assigned by mass spectrometry as YajC. A specific rotation of the periplasmic porter domain of AcrB is also revealed, consistent with the hypothesized "twist-to-open" mechanism for TolC activation. Growth experiments with yajc-deleted E. coli reveal a modest increase in the organism's susceptibility to beta-lactam antibiotics, but this effect could not conclusively be attributed to the loss of interactions between YajC and AcrB.

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author
; ; ; ; ; ; and
publishing date
type
Contribution to journal
publication status
published
keywords
Escherichia coli Proteins, Models, Molecular, Multidrug Resistance-Associated Proteins, Protein Conformation, Spectroscopy, Fourier Transform Infrared, Tandem Mass Spectrometry, X-Ray Diffraction, Journal Article, Research Support, Non-U.S. Gov't
in
Structure
volume
15
issue
12
pages
73 - 1663
publisher
Cell Press
external identifiers
  • scopus:36749071555
  • pmid:18073115
ISSN
0969-2126
DOI
10.1016/j.str.2007.09.023
language
English
LU publication?
no
id
d79ec04c-4e20-4e01-933e-a89937226839
date added to LUP
2017-04-29 15:32:30
date last changed
2024-04-14 09:34:01
@article{d79ec04c-4e20-4e01-933e-a89937226839,
  abstract     = {{<p>Bacterial drug resistance is a serious concern for human health. Multidrug efflux pumps export a broad variety of substrates out of the cell and thereby convey resistance to the host. In Escherichia coli, the AcrB:AcrA:TolC efflux complex forms a principal transporter for which structures of the individual component proteins have been determined in isolation. Here, we present the X-ray structure of AcrB in complex with a single transmembrane protein, assigned by mass spectrometry as YajC. A specific rotation of the periplasmic porter domain of AcrB is also revealed, consistent with the hypothesized "twist-to-open" mechanism for TolC activation. Growth experiments with yajc-deleted E. coli reveal a modest increase in the organism's susceptibility to beta-lactam antibiotics, but this effect could not conclusively be attributed to the loss of interactions between YajC and AcrB.</p>}},
  author       = {{Törnroth-Horsefield, Susanna and Gourdon, Pontus and Horsefield, Rob and Brive, Lars and Yamamoto, Natsuko and Mori, Hirotada and Snijder, Arjan and Neutze, Richard}},
  issn         = {{0969-2126}},
  keywords     = {{Escherichia coli Proteins; Models, Molecular; Multidrug Resistance-Associated Proteins; Protein Conformation; Spectroscopy, Fourier Transform Infrared; Tandem Mass Spectrometry; X-Ray Diffraction; Journal Article; Research Support, Non-U.S. Gov't}},
  language     = {{eng}},
  number       = {{12}},
  pages        = {{73--1663}},
  publisher    = {{Cell Press}},
  series       = {{Structure}},
  title        = {{Crystal structure of AcrB in complex with a single transmembrane subunit reveals another twist}},
  url          = {{http://dx.doi.org/10.1016/j.str.2007.09.023}},
  doi          = {{10.1016/j.str.2007.09.023}},
  volume       = {{15}},
  year         = {{2007}},
}