Crystallization of the bifunctional biotin operon repressor.

Published

Journal Article

The bifunctional birA gene product, BirA, which represses the biotin biosynthetic bio operon and also activates biotin in Escherichia coli, has been crystallized. The crystals have the tetragonal space group P4(1)2(1)2, or its enantiomorph, with unit cell dimensions a = b = 114.0 A and c = 60.2 A and diffract to at least 2.3 A resolution. The crystal packing requires that the monomers of the birA protein be arranged as dimers with two-fold symmetry. BirA is the first protein to be crystallized that is both a transcriptional regulator and an enzyme.

Full Text

Duke Authors

Cited Authors

  • Brennan, RG; Vasu, S; Matthews, BW; Otsuka, AJ

Published Date

  • January 5, 1989

Published In

Volume / Issue

  • 264 / 1

Start / End Page

  • 5 -

PubMed ID

  • 2642476

Pubmed Central ID

  • 2642476

International Standard Serial Number (ISSN)

  • 0021-9258

Language

  • eng

Conference Location

  • United States