Site-Directed Mutagenesis Reveals Putative Substrate Binding Residues in the Escherichia coli RND Efflux Pump AcrB
Site-Directed Mutagenesis Reveals Putative Substrate Binding Residues in the Escherichia coli RND Efflux Pump AcrB
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DOI：
10.1128/jb.00912-08
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发表时间：
2008-12-01
影响因子：
3.2
通讯作者：
Kern, Winfried V.
中科院分区：
文献类型：
--
作者：
Bohnert, Juergen A.;Schuster, Sabine;Kern, Winfried V.
大肠杆菌多药外排泵蛋白AcrB最近与多种底物共结晶，表明在F178和F615周围存在富含苯丙氨酸的结合位点。我们发现F610A是对底物mic影响最大的点突变，而其他靶向突变，包括苯丙氨酸136、178、615、617和628向丙氨酸的转化，其影响较小且更可变。
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.