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J Struct Biol. 2007 Sep;159(3):424-32. Epub 2007 May 16.

Crystal structure of a transcriptional regulator TM1030 from Thermotoga maritima solved by an unusual MAD experiment.

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Department of Molecular Physiology and Biological Physics, University of Virginia, 1340 Jefferson Park Avenue, Charlottesville, VA 22908, USA.


The crystal structure of a putative transcriptional regulator protein TM1030 from Thermotoga maritima, a hyperthermophilic bacterium, was determined by an unusual multi-wavelength anomalous dispersion method at 2.0 A resolution, in which data from two different crystals and two different beamlines were used. The protein belongs to the tetracycline repressor TetR superfamily. The three-dimensional structure of TM1030 is similar to the structures of proteins that function as multidrug-binding transcriptional repressors, and contains a large solvent-exposed pocket similar to the drug-binding pockets present in those repressors. The asymmetric unit in the crystal structure contains a single protein chain and the twofold symmetry of the dimer is adopted by the crystal symmetry. The structure described in this paper is an apo- form of TM1030. Although it is known that the protein is significantly overexpressed during heat shock, its detailed function cannot be yet explained.

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