1UTB
DntR from Burkholderia sp. strain DNT
Summary for 1UTB
Entry DOI | 10.2210/pdb1utb/pdb |
Descriptor | LYSR-TYPE REGULATORY PROTEIN, GLYCEROL, ACETATE ION, ... (5 entities in total) |
Functional Keywords | transcription regulation, lysr, transcriptional regulator |
Biological source | BURKHOLDERIA SP. More |
Total number of polymer chains | 2 |
Total formula weight | 71629.35 |
Authors | Smirnova, I.A.,Dian, C.,Leonard, G.A.,McSweeney, S.,Birse, D.,Brzezinski, P. (deposition date: 2003-12-05, release date: 2004-07-01, Last modification date: 2024-05-08) |
Primary citation | Smirnova, I.A.,Dian, C.,Leonard, G.A.,Mcsweeney, S.,Birse, D.,Brzezinski, P. Development of a Bacterial Biosensor for Nitrotoluenes: The Crystal Structure of the Transcriptional Regulator Dntr J.Mol.Biol., 340:405-, 2004 Cited by PubMed Abstract: The transcriptional regulator DntR, a member of the LysR family, is a central element in a prototype bacterial cell-based biosensor for the detection of hazardous contamination of soil and groundwater by dinitrotoluenes. To optimise the sensitivity of the biosensor for such compounds we have chosen a rational design of the inducer-binding cavity based on knowledge of the three-dimensional structure of DntR. We report two crystal structures of DntR with acetate (resolution 2.6 angstroms) and thiocyanate (resolution 2.3 angstroms), respectively, occupying the inducer-binding cavity. These structures allow for the construction of models of DntR in complex with salicylate (Kd approximately or = 4 microM) and 2,4-dinitrotoluene that provide a basis for the design of mutant DntR with enhanced specificity for dinitrotoluenes. In both crystal structures DntR crystallises as a homodimer with a "head-to-tail" arrangement of monomers in the asymmetric unit. Analysis of the crystal structure has allowed the building of a full-length model of DntR in its biologically active homotetrameric form consisting of two "head-to-head" dimers. The implications of this model for the mechanism of transcription regulation by LysR proteins are discussed. PubMed: 15210343DOI: 10.1016/J.JMB.2004.04.071 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.59 Å) |
Structure validation
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