Structural analysis of the purine repressor, an Escherichia coli DNA-binding protein.

Journal Article (Journal Article)

The purine repressor protein, PurR, is a member of the lac repressor, LacI, family of Escherichia coli DNA-binding proteins that bind DNA via a highly conserved N-terminal helix-turn-helix motif. Additionally, the members of this family display strong sequence homologies between their larger C-terminal effector binding/oligomerization domains. Analysis of the PurR primary and secondary structures reveals that its C-terminal corepressor binding domain is highly homologous to another group of E. coli-binding proteins, the periplasmic binding proteins, particularly to the ribose-binding protein (RBP). The high resolution x-ray structure of RBP allows this protein to serve as a template with which to model the predicted secondary structure of the corepressor binding domain of PurR. Similarly, the N-terminal DNA binding domain of PurR can be modeled using the NMR-determined structure of the corresponding region (residues 1-56) from LacI as a template. Combining the two, results in a description of the likely secondary structure topology of PurR and implicates residues important for corepressor binding and dimerization. CD spectroscopic studies on PurR, its corepressor binding domain and RBP result in secondary structure estimates nearly identical with those obtained by sequence analyses, thereby providing further corroborating physical evidence for this topological assignment.

Full Text

Duke Authors

Cited Authors

  • Schumacher, MA; Macdonald, JR; Björkman, J; Mowbray, SL; Brennan, RG

Published Date

  • June 15, 1993

Published In

Volume / Issue

  • 268 / 17

Start / End Page

  • 12282 - 12288

PubMed ID

  • 8509365

International Standard Serial Number (ISSN)

  • 0021-9258


  • eng

Conference Location

  • United States