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Crystallization of the bifunctional biotin operon repressor.

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.[1]

References

  1. Crystallization of the bifunctional biotin operon repressor. Brennan, R.G., Vasu, S., Matthews, B.W., Otsuka, A.J. J. Biol. Chem. (1989) [Pubmed]
 
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