1z77

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.