ArticleProceedings of the National Academy of Sciences of the United States of America2011
Structural contributions to multidrug recognition in the multidrug resistance (MDR) gene regulator, BmrR.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Determinants ofGenes · 2024Article
- A Specialized Polythioamide-Binding Protein Confers Antibiotic Self-Resistance in Anaerobic Bacteria.Angewandte Chemie (International ed. in English) · 2022Article
- Targeting the Holy Triangle of Quorum Sensing, Biofilm Formation, and Antibiotic Resistance in Pathogenic Bacteria.Microorganisms · 2022Review
- Chemotaxis of the Human Pathogen Pseudomonas aeruginosa to the Neurotransmitter Acetylcholine.mBio · 2022Article
- Bacterial MerR family transcription regulators: activationby distortion.Acta biochimica et biophysica Sinica · 2022Review
- Article
- Antibiotic binding releases autoinhibition of the TipA multidrug-resistance transcriptional regulator.The Journal of biological chemistry · 2020Article
- The bacterial multidrug resistance regulator BmrR distorts promoter DNA to activate transcription.Nature communications · 2020Article
- Reversal of doxorubicin resistance in lung cancer cells by neferine is explained by nuclear factor erythroid-derived 2-like 2 mediated lung resistance protein down regulation.Cancer drug resistance (Alhambra, Calif.) · 2020Article
- Emerging role of nuclear factor erythroid 2-related factor 2 in the mechanism of action and resistance to anticancer therapies.Cancer drug resistance (Alhambra, Calif.) · 2019Review
- Molecular insights into antibiotic resistance - how a binding protein traps albicidin.Nature communications · 2018Article
- BrlR from Pseudomonas aeruginosa is a receptor for both cyclic di-GMP and pyocyanin.Nature communications · 2018Article
- Broad blocking of MDR efflux pumps by acetylshikonin and acetoxyisovalerylshikonin to generate hypersensitive phenotype of malignant carcinoma cells.Scientific reports · 2018Article
- GyrI-like proteins catalyze cyclopropanoid hydrolysis to confer cellular protection.Nature communications · 2017Article
- Classification of ligand molecules in PDB with graph match-based structural superposition.Journal of structural and functional genomics · 2016Article
- Structural Analysis of the Hg(II)-Regulatory Protein Tn501 MerR from Pseudomonas aeruginosa.Scientific reports · 2016Article
- Antibiotic binding of STY3178, a yfdX protein from Salmonella Typhi.Scientific reports · 2016Article
- Transported substrate determines exchange rate in the multidrug resistance transporter EmrE.The Journal of biological chemistry · 2014Article
- Structures of a Na+-coupled, substrate-bound MATE multidrug transporter.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Plant Lessons: Exploring ABCB Functionality Through Structural Modeling.Frontiers in plant science · 2011Article
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4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Current views of multidrug (MD) recognition focus on large drug-binding cavities with flexible elements. However, MD recognition in BmrR is supported by a small, rigid drug-binding pocket. Here, a detailed description of MD binding by the noncanonical BmrR protein is offered through the combined use of X-ray and solution studies. Low shape complementarity, suboptimal packing, and efficient burial of a diverse set of ligands is facilitated by an aromatic docking platform formed by a set of conformationally fixed aromatic residues, hydrophobic pincer pair that locks the different drug structures on the adaptable platform surface, and a trio of acidic residues that enables cation selectivity without much regard to ligand structure. Within the binding pocket is a set of BmrR-derived H-bonding donor and acceptors that solvate a wide range of ligand polar substituent arrangements in a manner analogous to aqueous solvent. Energetic analyses of MD binding by BmrR are consistent with structural data. A common binding orientation for the different BmrR ligands is in line with promiscuous allosteric regulation.
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