2V57
Crystal structure of the TetR-like transcriptional regulator LfrR from Mycobacterium smegmatis in complex with proflavine
Summary for 2V57
| Entry DOI | 10.2210/pdb2v57/pdb |
| Related | 2WGB |
| Descriptor | TETR FAMILY TRANSCRIPTIONAL REPRESSOR LFRR, PROFLAVIN, ISOPROPYL ALCOHOL, ... (5 entities in total) |
| Functional Keywords | tetr, lfrr, repressor, dna-binding, transcription, transcription regulation |
| Biological source | MYCOBACTERIUM SMEGMATIS |
| Total number of polymer chains | 4 |
| Total formula weight | 83912.95 |
| Authors | Bellinzoni, M.,Buroni, S.,Riccardi, G.,De Rossi, E.,Alzari, P.M. (deposition date: 2008-10-02, release date: 2009-10-20, Last modification date: 2024-05-08) |
| Primary citation | Bellinzoni, M.,Buroni, S.,Schaeffer, F.,Riccardi, G.,De Rossi, E.,Alzari, P.M. Structural Plasticity and Distinct Drug-Binding Modes of Lfrr, a Mycobacterial Efflux Pump Regulator. J.Bacteriol., 191:7531-, 2009 Cited by PubMed Abstract: The TetR-like transcriptional repressor LfrR controls the expression of the gene encoding the Mycobacterium smegmatis efflux pump LfrA, which actively extrudes fluoroquinolones, cationic dyes, and anthracyclines from the cell and promotes intrinsic antibiotic resistance. The crystal structure of the apoprotein form of the repressor reveals a structurally asymmetric homodimer exhibiting local unfolding and a blocked drug-binding site, emphasizing the significant conformational plasticity of the protein necessary for DNA and multidrug recognition. Crystallographic and calorimetric studies of LfrR-drug complexes further confirm the intrinsic flexibility of the homodimer, which provides a dynamic mechanism to broaden multidrug binding specificity and may be a general property of transcriptional repressors regulating microbial efflux pump expression. PubMed: 19820093DOI: 10.1128/JB.00631-09 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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