1z77 | pdb_00001z77

Crystal structure of transcriptional regulator protein from Thermotoga maritima.

File:1z77.gif

spinqualitylabelsall models 1z77, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D

Overview

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.

About this Structure

1Z77 is a Single protein structure of sequence from Thermotoga maritima with EDO as ligand. Full crystallographic information is available from OCA.

Reference

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

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