3q5p

Crystal structure of BmrR bound to Tetracycline

spinqualitylabelsall models 3q5p, resolution 2.94Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3q5p is a 2 chain structure with sequence from "vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL, TAC Related: 3d6y, 3d6z, 3q1m, 3q2y, 3q5r, 3q5s Gene: bmrR, bmr1R, BSU24020 ("Vibrio subtilis" Ehrenberg 1835) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [BMRR_BACSU] Activates transcription of the bmr gene in response to structurally dissimilar drugs. Binds rhodamine as an inducer. Publication Abstract from PubMed 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. Structural contributions to multidrug recognition in the multidrug resistance (MDR) gene regulator, BmrR.,Bachas S, Eginton C, Gunio D, Wade H Proc Natl Acad Sci U S A. 2011 Jul 5;108(27):11046-51. Epub 2011 Jun 20. PMID:21690368 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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