Crystal Structure of AcrB in Complex with a Single Transmembrane Subunit Reveals Another Twist.
Journal article, 2007

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.



Susanna Törnroth-Horsefield

University of Gothenburg

Pontus Emanuel Gourdon

Chalmers, Chemical and Biological Engineering, Molecular Biotechnology

Rob Horsefield

University of Gothenburg

Lars Brive

University of Gothenburg

Natsuko Yamamoto

Nara Institute of Science and Technology

Hirotada Mori

Nara Institute of Science and Technology

Arjan Snijder

Chalmers, Chemical and Biological Engineering, Molecular Biotechnology

Richard Neutze

University of Gothenburg


0969-2126 (ISSN)

Vol. 15 12 1663-73

Subject Categories

Structural Biology

Bioinformatics and Systems Biology





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