Conformational changes of purine repressor DNA-binding domain upon complexation with DNA.

Published

Journal Article

The purine repressor (PurR) consists of two functional domains: an N-terminal DNA-binding domain and a C-terminal corepressor-binding domain. Recently, the structure of PurR-corepressor-operator ternary complex was determined by X-ray crystallography. In the complex the DNA-binding domain, consisting of 56 amino acids, was composed of four helices. Here, we have determined the solution structure of the DNA-binding domain in its DNA free state by NMR. It consists of three helices and the fourth helix (the hinge helix) region is diordered. The architecture of the first three helices of its DNA free state is very similar to that of its DNA-bound form. The hinge helix is induced by the specific DNA binding and by the dimerization of PurR which is provided by the corepressor-binding domain.

Full Text

Duke Authors

Cited Authors

  • Nagadoi, A; Nakazawa, K; Morikawa, S; Nakamura, H; Sampei, G; Mizobuchi, K; Yamamoto, H; Schumacher, MA; Brennan, RG; Nishimura, Y

Published Date

  • 1995

Published In

Start / End Page

  • 63 - 64

PubMed ID

  • 8841553

Pubmed Central ID

  • 8841553

International Standard Serial Number (ISSN)

  • 0261-3166

Language

  • eng

Conference Location

  • England