期刊
ANTIMICROBIAL AGENTS AND CHEMOTHERAPY
卷 58, 期 8, 页码 4767-4772出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/AAC.02733-13
关键词
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资金
- German Research Foundation Collaborative Center [SFB807]
- German Research Foundation Cluster of Excellence [EXC115]
- Innovative Medicines Initiative (IMI) Joint Undertaking project Translocation
Multidrug efflux transporters recognize a variety of structurally unrelated compounds for which the molecular basis is poorly understood. For the resistance nodulation and cell division (RND) inner membrane component AcrB of the AcrAB-TolC multidrug efflux system from Escherichia coli, drug binding occurs at the access and deep binding pockets. These two binding areas are separated by an 11-amino-acid-residue-containing switch loop whose conformational flexibility is speculated to be essential for drug binding and transport. A G616N substitution in the switch loop has a distinct and local effect on the orientation of the loop and on the ability to transport larger drugs. Here, we report a distinct phenotypical pattern of drug recognition and transport for the G616N variant, indicating that drug substrates with minimal projection areas of >= 70 angstrom(2) are less well transported than other substrates.
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