title: Lac repressor-operator complex.
abstract: For many years the lac operon of Escherichia coli has been the paradigm for gene regulation. Recently, the structures of the lac repressor core bound to isopropyl-beta-D-1-thiogalactoside (IPTG), the intact apo lac repressor, the intact lac repressor complexes with IPTG and a 21-base-pair symmetric operator, and the refined headpiece of the repressor have been determined. These structures have provided a framework for understanding a wealth of biochemical and genetic information. An analysis of these structures, as well as a description of their function and a comparison to homologous proteins, is now possible.
authors.affiliation: Department of Chemistry, University of Pennsylvania, Philadelphia, PA 19104, USA. kercher@crystal.med.upenn.edu
authors.forename: M A
authors.initials: MA
authors.lastname: Kercher
authors.forename: P
authors.initials: P
authors.lastname: Lu
authors.forename: M
authors.initials: M
authors.lastname: Lewis
mesh_terms: D000494:Allosteric Regulation; D001426:Bacterial Proteins / Q000378:metabolism*; D001665:Binding Sites; D029968:Escherichia coli Proteins; D007763:Lac Operon; D056968:Lac Repressors; D011485:Protein Binding; D012097:Repressor Proteins / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D056968:Lac Repressors; D012097:Repressor Proteins