1UTH

DntR from Burkholderia sp. strain DNT in complex with Thiocyanate

Summary for 1UTH

• Entry DOI: 10.2210/pdb1uth/pdb
• Related: 1UTB
• Descriptor: LYSR-TYPE REGULATORY PROTEIN, THIOCYANATE ION, ... (4 entities in total)
• Functional Keywords: transcription regulation, lysr, transcriptional regulator
• Biological source: BURKHOLDERIA SP.; More
• Total number of polymer chains: 2
• Total formula weight: 72022.26

Authors

Smirnova, I.A.,Dian, C.,Leonard, G.A.,McSweeney, S.,Birse, D.,Brzezinski, P. (deposition date: 2003-12-09, release date: 2004-07-01, Last modification date: 2023-12-13)

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

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: 15210343
DOI: 10.1016/J.JMB.2004.04.071

Experimental method

X-RAY DIFFRACTION (2.2 Å)