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. 2007 Mar 16;367(1):102-12. doi: 10.1016/j.jmb.2006.12.018. Epub 2006 Dec 12.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acids, Aromatic / biosynthesis*
  • Biological Transport / physiology*
  • Crystallography
  • Databases, Protein
  • Escherichia coli K12 / metabolism*
  • Escherichia coli Proteins / chemistry*
  • Protein Conformation
  • Protein Structure, Tertiary
  • Repressor Proteins / chemistry*
  • Transcription Factors / chemistry*
  • Transcription Factors / physiology
  • Transcription, Genetic


  • Amino Acids, Aromatic
  • Escherichia coli Proteins
  • Repressor Proteins
  • Transcription Factors
  • TyrR protein, E coli

Associated data

  • PDB/EBI-30882