Literature DB >> 2642476

Crystallization of the bifunctional biotin operon repressor.

R G Brennan1, S Vasu, B W Matthews, A J Otsuka.   

Abstract

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.

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Year:  1989        PMID： 2642476

Source DB:  PubMed          Journal:  J Biol Chem        ISSN： 0021-9258            Impact factor:   5.157


  2 in total

1.  Corepressor-induced organization and assembly of the biotin repressor: a model for allosteric activation of a transcriptional regulator.

Authors:  L H Weaver; K Kwon; D Beckett; B W Matthews
Journal:  Proc Natl Acad Sci U S A       Date:  2001-05-15       Impact factor: 11.205

2.  Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domains.

Authors:  K P Wilson; L M Shewchuk; R G Brennan; A J Otsuka; B W Matthews
Journal:  Proc Natl Acad Sci U S A       Date:  1992-10-01       Impact factor: 11.205
  2 in total

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