Crystallization of the bifunctional biotin operon repressor.
Publication
, Journal Article
Brennan, RG; Vasu, S; Matthews, BW; Otsuka, AJ
Published in: J Biol Chem
January 5, 1989
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.
Duke Scholars
Published In
J Biol Chem
ISSN
0021-9258
Publication Date
January 5, 1989
Volume
264
Issue
1
Start / End Page
5
Location
United States
Related Subject Headings
- Transcription Factors
- Repressor Proteins
- Protein Conformation
- Operon
- Macromolecular Substances
- Escherichia coli Proteins
- Escherichia coli
- Crystallization
- Carbon-Nitrogen Ligases
- Biotin
Citation
APA
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ICMJE
MLA
NLM
Brennan, R. G., Vasu, S., Matthews, B. W., & Otsuka, A. J. (1989). Crystallization of the bifunctional biotin operon repressor. J Biol Chem, 264(1), 5.
Brennan, R. G., S. Vasu, B. W. Matthews, and A. J. Otsuka. “Crystallization of the bifunctional biotin operon repressor.” J Biol Chem 264, no. 1 (January 5, 1989): 5.
Brennan RG, Vasu S, Matthews BW, Otsuka AJ. Crystallization of the bifunctional biotin operon repressor. J Biol Chem. 1989 Jan 5;264(1):5.
Brennan, R. G., et al. “Crystallization of the bifunctional biotin operon repressor.” J Biol Chem, vol. 264, no. 1, Jan. 1989, p. 5.
Brennan RG, Vasu S, Matthews BW, Otsuka AJ. Crystallization of the bifunctional biotin operon repressor. J Biol Chem. 1989 Jan 5;264(1):5.
Published In
J Biol Chem
ISSN
0021-9258
Publication Date
January 5, 1989
Volume
264
Issue
1
Start / End Page
5
Location
United States
Related Subject Headings
- Transcription Factors
- Repressor Proteins
- Protein Conformation
- Operon
- Macromolecular Substances
- Escherichia coli Proteins
- Escherichia coli
- Crystallization
- Carbon-Nitrogen Ligases
- Biotin