3FRQ
Structure of the macrolide biosensor protein, MphR(A), with erythromcyin
Summary for 3FRQ
| Entry DOI | 10.2210/pdb3frq/pdb |
| Descriptor | Repressor protein MphR(A), ERYTHROMYCIN A, GLYCEROL, ... (5 entities in total) |
| Functional Keywords | macrolide antibiotic. repressor, biosensor, erythromycin, strptomyces, natural products, biosynthesis, dna-binding, transcription, transcription regulation, dna binding protein |
| Biological source | Escherichia coli |
| Total number of polymer chains | 2 |
| Total formula weight | 45511.70 |
| Authors | Zheng, J.,Sagar, V.,Smolinsky, A.,Bourke, C.,LaRonde-LeBlanc, N.,Cropp, T.A. (deposition date: 2009-01-08, release date: 2009-03-24, Last modification date: 2024-02-21) |
| Primary citation | Zheng, J.,Sagar, V.,Smolinsky, A.,Bourke, C.,LaRonde-LeBlanc, N.,Cropp, T.A. Structure and function of the macrolide biosensor protein, MphR(A), with and without erythromycin J.Mol.Biol., 387:1250-1260, 2009 Cited by PubMed Abstract: The regulatory protein MphR(A) has recently seen extensive use in synthetic biological applications, such as metabolite sensing and exogenous control of gene expression. This protein negatively regulates the expression of a macrolide 2'-phosphotransferase I resistance gene (mphA) via binding to a 35-bp DNA operator upstream of the start codon and is de-repressed by the presence of erythromycin. Here, we present the refined crystal structure of the MphR(A) protein free of erythromycin and that of the MphR(A) protein with bound erythromycin at 2.00- and 1.76-A resolutions, respectively. We also studied the DNA binding properties of the protein and identified mutants of MphR(A) that are defective in gene repression and ligand binding in a cell-based reporter assay. The combination of these two structures illustrates the molecular basis of erythromycin-induced gene expression and provides a framework for additional applied uses of this protein in the isolation and engineered biosynthesis of polyketide natural products. PubMed: 19265703DOI: 10.1016/j.jmb.2009.02.058 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.76 Å) |
Structure validation
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