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Crystallization and preliminary X-ray studies on the co-repressor binding domain of the Escherichia coli purine repressor.

Publication ,  Journal Article
Schumacher, MA; Choi, KY; Zalkin, H; Brennan, RG
Published in: J Mol Biol
June 20, 1992

The purine repressor is a putative helix-turn-helix DNA-binding protein that regulates several genetic loci important in purine and pyrimidine metabolism in Escherichia coli. The protein is composed of two domains, an N-terminal DNA-binding domain and a C-terminal core that binds the purine co-repressors, guanine and hypoxanthine. The co-repressor binding domain (residues 53 to 341) has been crystallized from polyethylene glycol 600-MgCl2 solutions. They are of the monoclinic form, space group P2(1), with a = 38.2 A, b = 125.7 A, c = 61.8 A and beta = 100.2 degrees. They diffract to a resolution of at least 2.2 A and contain two monomers per asymmetric unit. The importance of the structural determination of this domain is underscored by the high degree of sequence homology displayed within the effector binding sites among a sub-class of helix-turn-helix proteins, of which LacI and GalR are members. The structure of the PurR co-repressor binding domain will provide a high resolution view of one such domain and could serve as a possible model for future effector site structural determinations. Perhaps more important will be this structure's contribution to the further understanding of how protein-DNA interactions are modulated.

Duke Scholars

Published In

J Mol Biol

DOI

ISSN

0022-2836

Publication Date

June 20, 1992

Volume

225

Issue

4

Start / End Page

1131 / 1133

Location

Netherlands

Related Subject Headings

  • X-Ray Diffraction
  • Repressor Proteins
  • Protein Conformation
  • Escherichia coli Proteins
  • Escherichia coli
  • DNA-Binding Proteins
  • Biochemistry & Molecular Biology
  • Binding Sites
  • Bacterial Proteins
  • 0605 Microbiology
 

Citation

APA
Chicago
ICMJE
MLA
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Schumacher, M. A., Choi, K. Y., Zalkin, H., & Brennan, R. G. (1992). Crystallization and preliminary X-ray studies on the co-repressor binding domain of the Escherichia coli purine repressor. J Mol Biol, 225(4), 1131–1133. https://doi.org/10.1016/0022-2836(92)90111-v
Schumacher, M. A., K. Y. Choi, H. Zalkin, and R. G. Brennan. “Crystallization and preliminary X-ray studies on the co-repressor binding domain of the Escherichia coli purine repressor.J Mol Biol 225, no. 4 (June 20, 1992): 1131–33. https://doi.org/10.1016/0022-2836(92)90111-v.
Schumacher MA, Choi KY, Zalkin H, Brennan RG. Crystallization and preliminary X-ray studies on the co-repressor binding domain of the Escherichia coli purine repressor. J Mol Biol. 1992 Jun 20;225(4):1131–3.
Schumacher, M. A., et al. “Crystallization and preliminary X-ray studies on the co-repressor binding domain of the Escherichia coli purine repressor.J Mol Biol, vol. 225, no. 4, June 1992, pp. 1131–33. Pubmed, doi:10.1016/0022-2836(92)90111-v.
Schumacher MA, Choi KY, Zalkin H, Brennan RG. Crystallization and preliminary X-ray studies on the co-repressor binding domain of the Escherichia coli purine repressor. J Mol Biol. 1992 Jun 20;225(4):1131–1133.
Journal cover image

Published In

J Mol Biol

DOI

ISSN

0022-2836

Publication Date

June 20, 1992

Volume

225

Issue

4

Start / End Page

1131 / 1133

Location

Netherlands

Related Subject Headings

  • X-Ray Diffraction
  • Repressor Proteins
  • Protein Conformation
  • Escherichia coli Proteins
  • Escherichia coli
  • DNA-Binding Proteins
  • Biochemistry & Molecular Biology
  • Binding Sites
  • Bacterial Proteins
  • 0605 Microbiology