The crystal structure of multidrug-resistance regulator RamR with multiple drugs

Suguru Yamasaki, Eiji Nikaido, Ryosuke Nakashima, Keisuke Sakurai, Daisuke Fujiwara, Ikuo Fujii and Kunihiko Nishino ()
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Suguru Yamasaki: Laboratory of Microbiology and Infectious Diseases, Institute of Scientific and Industrial Research, Osaka University
Eiji Nikaido: Laboratory of Microbiology and Infectious Diseases, Institute of Scientific and Industrial Research, Osaka University
Ryosuke Nakashima: Laboratory of Cell Membrane Structure Biology, Institute of Scientific and Industrial Research, Osaka University
Keisuke Sakurai: Laboratory of Cell Membrane Structure Biology, Institute of Scientific and Industrial Research, Osaka University
Daisuke Fujiwara: Graduate School of Science, Osaka Prefecture University
Ikuo Fujii: Graduate School of Science, Osaka Prefecture University
Kunihiko Nishino: Laboratory of Microbiology and Infectious Diseases, Institute of Scientific and Industrial Research, Osaka University

Nature Communications, 2013, vol. 4, issue 1, 1-7

Abstract: Abstract RamR is a transcriptional repressor of the gene-encoding RamA protein, which controls the expression of the multidrug efflux system genes acrAB-tolC. RamR is an important multidrug-resistance factor, however, its structure and the identity of the molecules to which it responds have been unknown. Here, we report the crystal structure of RamR in complex with multiple drugs, including berberine, crystal violet, dequalinium, ethidium bromide and rhodamine 6G. All compounds are found to interact with Phe155 of RamR, and each compound is surrounded by different amino acid residues. Binding of these compounds to RamR reduces its DNA-binding affinity, which results in the increased expression of ramA. Our results reveal significant flexibility in the substrate-recognition region of RamR, which regulates the bacterial efflux participating in multidrug resistance.

Date: 2013
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DOI: 10.1038/ncomms3078

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