A protein structure from nuclear magnetic resonance data. lac repressor headpiece.
A procedure is described to determine the three-dimensional structure of biomolecules from nuclear magnetic resonance data. This procedure combines model building with a restrained molecular dynamics algorithm, in which distance information from nuclear Overhauser effects is incorporated in the form of pseudo potentials. The method has been applied to the N-terminal DNA-binding domain or headpiece (amino acid residues 1 to 51) of the lac repressor from Escherichia coli, for which no crystal structure is available. The relative orientation of the three helices of the headpiece is similar to that of the three homologous helices found in the cI repressor of bacteriophage lambda.
D000595:Amino Acid Sequence; D004926:Escherichia coli / Q000032:analysis*; D009682:Magnetic Resonance Spectroscopy; D011487:Protein Conformation; D012097:Repressor Proteins; D014157:Transcription Factors
D012097:Repressor Proteins; D014157:Transcription Factors