1uth
From Proteopedia
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==Overview== | ==Overview== | ||
| - | 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 ... | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1UTH is a | + | 1UTH is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Burkholderia_sp. Burkholderia sp.] with SCN as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UTH OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transcriptional regulator]] | [[Category: transcriptional regulator]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 13:07:37 2007'' |
Revision as of 11:02, 5 November 2007
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DNTR FROM BURKHOLDERIA SP. STRAIN DNT IN COMPLEX WITH THIOCYANATE
Overview
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.
About this Structure
1UTH is a Protein complex structure of sequences from Burkholderia sp. with SCN as ligand. Structure known Active Site: AC1. Full crystallographic information is available from OCA.
Reference
Development of a bacterial biosensor for nitrotoluenes: the crystal structure of the transcriptional regulator DntR., Smirnova IA, Dian C, Leonard GA, McSweeney S, Birse D, Brzezinski P, J Mol Biol. 2004 Jul 9;340(3):405-18. PMID:15210343
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