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1Z77

Crystal structure of transcriptional regulator protein from Thermotoga maritima.

Summary for 1Z77
Entry DOI10.2210/pdb1z77/pdb
Descriptortranscriptional regulator (TetR family), 1,2-ETHANEDIOL (3 entities in total)
Functional Keywordstranscriptional regulator, tetr family, structural genomics, psi, protein structure initiative, midwest center for structural genomics, mcsg, transcription
Biological sourceThermotoga maritima
Total number of polymer chains1
Total formula weight24338.01
Authors
Koclega, K.D.,Chruszcz, M.,Zimmerman, M.D.,Cymborowski, M.,Kudritska, M.,Minor, W.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2005-03-24, release date: 2005-05-10, Last modification date: 2024-11-20)
Primary citationKoclega, K.D.,Chruszcz, M.,Zimmerman, M.D.,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., 159:424-432, 2007
Cited by
PubMed Abstract: 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.
PubMed: 17588774
DOI: 10.1016/j.jsb.2007.04.012
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

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