Lac repressor at last.
Crystal and cocrystal structures of the LacI and PurR repressors reveal a novel use of hinge alpha helices which bind in the minor groove of the operator and mediate transmission of the allosteric signals that modulate DNA-binding activity.
Sauer
R T
RT
Department of Biology, MIT, Cambridge, MA 02139, USA.
D001426:Bacterial Proteins / Q000737:chemistry* / Q000502:physiology; D001665:Binding Sites; D018360:Crystallography, X-Ray; D029968:Escherichia coli Proteins; D007763:Lac Operon; D056968:Lac Repressors; D008958:Models, Molecular; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D012097:Repressor Proteins / Q000737:chemistry* / Q000502:physiology; D014158:Transcription, Genetic
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D056968:Lac Repressors; C065825:PurR protein, Bacteria; C489317:PurR protein, E coli; D012097:Repressor Proteins