Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Crystal structure of a transcriptional regulator TM1030 from Thermotoga maritima solved by an unusual MAD experiment.,Koclega KD, Chruszcz M, Zimmerman MD, Cymborowski M, Evdokimova E, Minor W J Struct Biol. 2007 Sep;159(3):424-32. Epub 2007 May 16. PMID:17588774[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Koclega KD, Chruszcz M, Zimmerman MD, Cymborowski M, Evdokimova E, Minor W. Crystal structure of a transcriptional regulator TM1030 from Thermotoga maritima solved by an unusual MAD experiment. J Struct Biol. 2007 Sep;159(3):424-32. Epub 2007 May 16. PMID:17588774 doi:10.1016/j.jsb.2007.04.012
