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.
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.
Verger
D
D
School of Crystallography, Birkbeck College, University of London, UK.
Carr
P D
PD
Kwok
T
T
Ollis
D L
DL
D024322:Amino Acids, Aromatic / Q000096:biosynthesis*; D001692:Biological Transport / Q000502:physiology*; D003461:Crystallography; D030562:Databases, Protein; D048168:Escherichia coli K12 / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry*; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D012097:Repressor Proteins / Q000737:chemistry*; D014157:Transcription Factors / Q000737:chemistry* / Q000502:physiology; D014158:Transcription, Genetic
D024322:Amino Acids, Aromatic; D029968:Escherichia coli Proteins; D012097:Repressor Proteins; D014157:Transcription Factors; C069256:TyrR protein, E coli