Two-dimensional NMR study of a protein-DNA complex. lac repressor headpiece-operator interaction

R Kaptein, R M Lamerichs, R Boelens, J A Rullmann

Research output: Contribution to journalArticleAcademicpeer-review


The interaction of the N-terminal DNA-binding domain (56 amino acid residues) of the lac repressor with lac operator DNA was analyzed using two-dimensional NMR spectroscopy. Both half-operators (11 and 14 bp) and a complete fully symmetric 22 bp operator were studied. Two-dimensional nuclear Overhauser effect (2D NOE) spectra of headpiece-operator complexes were taken in both D2O and H2O solutions. Special attention was given to the problem of 1H resonance assignments. Based on an analysis of the proton-proton NOEs, a model for the headpiece-operator complex could be derived. In this model, most of the protein-DNA contracts occur between amino acid residues in the second helix (recognition helix) of the lac headpiece and DNA bases in the major groove. The orientation of this helix with respect to the dyad axis of the operator is opposite to that found in the X-ray structures of several other repressor-operator complexes.

Original languageEnglish
Pages (from-to)89-96
Number of pages8
JournalBiochemical Pharmacology
Issue number1
Publication statusPublished - 1 Jul 1990


  • Base Composition
  • Base Sequence
  • DNA
  • Magnetic Resonance Spectroscopy
  • Models, Molecular
  • Molecular Sequence Data
  • Operator Regions, Genetic
  • Pattern Recognition, Automated
  • Peptide Fragments
  • Protein Conformation
  • Repressor Proteins
  • Structure-Activity Relationship
  • Transcription Factors


Dive into the research topics of 'Two-dimensional NMR study of a protein-DNA complex. lac repressor headpiece-operator interaction'. Together they form a unique fingerprint.

Cite this