Crystal structure of a transcriptional regulator TM1030 from Thermotoga maritima solved by an unusual MAD experiment.
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.
Koclega
Katarzyna D
KD
Department of Molecular Physiology and Biological Physics, University of Virginia, 1340 Jefferson Park Avenue, Charlottesville, VA 22908, USA.
Chruszcz
Maksymilian
M
Zimmerman
Matthew D
MD
Cymborowski
Marcin
M
Evdokimova
Elena
E
Minor
Wladek
W
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D003461:Crystallography / Q000379:methods*; D004247:DNA / Q000737:chemistry; D008969:Molecular Sequence Data; D011487:Protein Conformation; D016415:Sequence Alignment; D020124:Thermotoga maritima / Q000378:metabolism*; D015534:Trans-Activators / Q000737:chemistry* / Q000235:genetics
D001426:Bacterial Proteins; D015534:Trans-Activators; D004247:DNA