Article
Structural and biochemical characterization of MepR, a multidrug binding transcription regulator of the Staphylococcus aureus multidrug efflux pump MepA.
Nucleic acids research - 1 Mar 2009
Kumaraswami Muthiah, Schuman Jason T, Seo Susan M, Kaatz Glenn W, Brennan Richard G
Abstract excerpt
MepR is a multidrug binding transcription regulator that represses expression of the Staphylococcus aureus multidrug efflux pump gene, mepA, as well as its own gene. MepR is induced by multiple cationic toxins, which are also substrates of MepA. In order to understand the gene regulatory and drug-binding mechanisms of MepR, we carried out biochemical, in vivo and structural studies. The 2.40 A resolution...
Topics
- Amino Acid Sequence
- Bacterial Proteins
- Crystallography, X-Ray
- DNA, Bacterial
- DNA-Binding Proteins
- Ethidium
- Indoles
- Membrane Transport Proteins
- Models, Molecular
- Molecular Sequence Data
- Mutation
- Operator Regions, Genetic
- Protein Structure, Secondary