Permanent URL to this publication: http://dx.doi.org/10.5167/uzh-6288
Bohnert, J A; Schuster, S; Seeger, M A; Fähnrich, E; Pos, K M; Kern, W V (2008). Site-directed mutagenesis reveals putative substrate binding residues in the escherichia coli RND efflux pump AcrB. Journal of Bacteriology, 190(24):8225-8229.
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.
|Item Type:||Journal Article, refereed, original work|
|Communities & Collections:||04 Faculty of Medicine > Center for Integrative Human Physiology|
04 Faculty of Medicine > Institute of Physiology
07 Faculty of Science > Institute of Physiology
|DDC:||570 Life sciences; biology|
610 Medicine & health
|Deposited On:||02 Dec 2008 12:19|
|Last Modified:||27 Nov 2013 22:56|
|Publisher:||American Society for Microbiology|
|Additional Information:||Copyright: American Society for Microbiology|
|Citations:||Web of Science®. Times Cited: 33|
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