Skip to main content
Journal cover image

Crystal structure of the lactose operon repressor and its complexes with DNA and inducer.

Publication ,  Journal Article
Lewis, M; Chang, G; Horton, NC; Kercher, MA; Pace, HC; Schumacher, MA; Brennan, RG; Lu, P
Published in: Science
March 1, 1996

The lac operon of Escherichia coli is the paradigm for gene regulation. Its key component is the lac repressor, a product of the lacI gene. The three-dimensional structures of the intact lac repressor, the lac repressor bound to the gratuitous inducer isopropyl-beta-D-1-thiogalactoside (IPTG) and the lac repressor complexed with a 21-base pair symmetric operator DNA have been determined. These three structures show the conformation of the molecule in both the induced and repressed states and provide a framework for understanding a wealth of biochemical and genetic information. The DNA sequence of the lac operon has three lac repressor recognition sites in a stretch of 500 base pairs. The crystallographic structure of the complex with DNA suggests that the tetrameric repressor functions synergistically with catabolite gene activator protein (CAP) and participates in the quaternary formation of repression loops in which one tetrameric repressor interacts simultaneously with two sites on the genomic DNA.

Duke Scholars

Altmetric Attention Stats
Dimensions Citation Stats

Published In

Science

DOI

ISSN

0036-8075

Publication Date

March 1, 1996

Volume

271

Issue

5253

Start / End Page

1247 / 1254

Location

United States

Related Subject Headings

  • Repressor Proteins
  • Protein Structure, Secondary
  • Protein Folding
  • Protein Conformation
  • Point Mutation
  • Operator Regions, Genetic
  • Nucleic Acid Conformation
  • Molecular Sequence Data
  • Models, Molecular
  • Lac Repressors
 

Citation

APA
Chicago
ICMJE
MLA
NLM
Lewis, M., Chang, G., Horton, N. C., Kercher, M. A., Pace, H. C., Schumacher, M. A., … Lu, P. (1996). Crystal structure of the lactose operon repressor and its complexes with DNA and inducer. Science, 271(5253), 1247–1254. https://doi.org/10.1126/science.271.5253.1247
Lewis, M., G. Chang, N. C. Horton, M. A. Kercher, H. C. Pace, M. A. Schumacher, R. G. Brennan, and P. Lu. “Crystal structure of the lactose operon repressor and its complexes with DNA and inducer.Science 271, no. 5253 (March 1, 1996): 1247–54. https://doi.org/10.1126/science.271.5253.1247.
Lewis M, Chang G, Horton NC, Kercher MA, Pace HC, Schumacher MA, et al. Crystal structure of the lactose operon repressor and its complexes with DNA and inducer. Science. 1996 Mar 1;271(5253):1247–54.
Lewis, M., et al. “Crystal structure of the lactose operon repressor and its complexes with DNA and inducer.Science, vol. 271, no. 5253, Mar. 1996, pp. 1247–54. Pubmed, doi:10.1126/science.271.5253.1247.
Lewis M, Chang G, Horton NC, Kercher MA, Pace HC, Schumacher MA, Brennan RG, Lu P. Crystal structure of the lactose operon repressor and its complexes with DNA and inducer. Science. 1996 Mar 1;271(5253):1247–1254.
Journal cover image

Published In

Science

DOI

ISSN

0036-8075

Publication Date

March 1, 1996

Volume

271

Issue

5253

Start / End Page

1247 / 1254

Location

United States

Related Subject Headings

  • Repressor Proteins
  • Protein Structure, Secondary
  • Protein Folding
  • Protein Conformation
  • Point Mutation
  • Operator Regions, Genetic
  • Nucleic Acid Conformation
  • Molecular Sequence Data
  • Models, Molecular
  • Lac Repressors