2JHE
N-terminal domain of TyrR transcription factor (residues 1 - 190)
Summary for 2JHE
Entry DOI | 10.2210/pdb2jhe/pdb |
Descriptor | TRANSCRIPTION REGULATOR TYRR, 2-(2-ETHOXYETHOXY)ETHANOL, TETRAETHYLENE GLYCOL, ... (5 entities in total) |
Functional Keywords | transcription, aromatic hydrocarbons catabolism, tyrr protein, nucleotide-binding, transcription regulation, activator, repressor, atp-binding, dna-binding, two-component regulatory system |
Biological source | ESCHERICHIA COLI |
Total number of polymer chains | 4 |
Total formula weight | 87514.68 |
Authors | Verger, D.,Carr, P.D.,Kwok, T.,Ollis, D.L. (deposition date: 2007-02-21, release date: 2008-06-24, Last modification date: 2024-05-08) |
Primary citation | Verger, D.,Carr, P.D.,Kwok, T.,Ollis, D.L. Crystal Structure of the N-Terminal Domain of the Tyrr Transcription Factor Responsible for Gene Regulation of Aromatic Amino Acid Biosynthesis and Transport in Escherichia Coli K12 J.Mol.Biol., 367:102-, 2007 Cited by PubMed Abstract: The X-ray structure of the N-terminal domain of TyrR has been solved to a resolution of 2.3 A. It reveals a modular protein containing an ACT domain, a connecting helix, a PAS domain and a C-terminal helix. Two dimers are present in the asymmetric unit with one monomer of each pair exhibiting a large rigid-body movement that results in a hinging around residue 74 of approximately 50 degrees . The structure of the dimer is discussed with reference to other transcription regulator proteins. Putative binding sites are identified for the aromatic amino acid cofactors. PubMed: 17222426DOI: 10.1016/J.JMB.2006.12.018 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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