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Journal of Bacteriology, December 2008, p. 8225-8229, Vol. 190, No. 24
0021-9193/08/$08.00+0 doi:10.1128/JB.00912-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Center for Infectious Diseases and Travel Medicine, University Hospital, and Department of Medicine, Albert Ludwigs University, Freiburg, Germany,1 Institute of Physiology and Zürich Centre for Integrative Human Physiology, University of Zürich, Zürich, Switzerland2
Received 2 July 2008/ Accepted 1 October 2008
The Escherichia coli multidrug efflux pump protein AcrB has recently been cocrystallized with various substrates, suggesting that there is a phenylalanine-rich binding site around F178 and F615. We found that F610A was the point mutation that had the most significant impact on substrate MICs, while other targeted mutations, including conversion of phenylalanines 136, 178, 615, 617, and 628 to alanine, had smaller and more variable effects.
Published ahead of print on 10 October 2008.
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