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Site-directed mutagenesis reveals putative substrate binding residues in the escherichia coli RND efflux pump AcrB


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.

Abstract

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.

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.

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Additional indexing

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
Dewey Decimal Classification:570 Life sciences; biology
610 Medicine & health
Language:English
Date:2008
Deposited On:02 Dec 2008 11:19
Last Modified:05 Apr 2016 12:36
Publisher:American Society for Microbiology
ISSN:0021-9193
Additional Information:Copyright: American Society for Microbiology
Publisher DOI:10.1128/JB.00912-08
PubMed ID:18849422
Permanent URL: http://doi.org/10.5167/uzh-6288

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