3Q5R
Crystal structure of BmrR bound to Kanamycin
Summary for 3Q5R
| Entry DOI | 10.2210/pdb3q5r/pdb |
| Related | 3D6Y 3D6Z |
| Descriptor | Multidrug-efflux transporter 1 regulator, 23 bp promoter DNA, KANAMYCIN A (3 entities in total) |
| Functional Keywords | multidrug binding, multidrug resistance, transcription regulator, transcription-rna-antibiotic complex, transcription/rna/antibiotic |
| Biological source | Bacillus subtilis More |
| Total number of polymer chains | 2 |
| Total formula weight | 41021.24 |
| Authors | Bachas, S.,Eginton, C.,Gunio, G.,Wade, H. (deposition date: 2010-12-29, release date: 2011-07-20, Last modification date: 2024-02-21) |
| Primary citation | Bachas, S.,Eginton, C.,Gunio, D.,Wade, H. Structural contributions to multidrug recognition in the multidrug resistance (MDR) gene regulator, BmrR. Proc.Natl.Acad.Sci.USA, 108:11046-11051, 2011 Cited by PubMed 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. PubMed: 21690368DOI: 10.1073/pnas.1104850108 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.05 Å) |
Structure validation
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