PMID:8089849
| Citation |
Schumacher, MA, Choi, KY, Zalkin, H and Brennan, RG (1994) Crystallization and preliminary X-ray analysis of an Escherichia coli purine repressor-hypoxanthine-DNA complex. J. Mol. Biol. 242:302-5 |
|---|---|
| Abstract |
The purine repressor (PurR) is a DNA-binding protein, which together with a purine corepressor serves to regulate de novo purine and pyrimidine biosynthesis in Escherichia coli. PurR belongs to the structurally homologous lac repressor family of transcription regulators. A PurR-hypoxanthine-DNA complex has been crystallized, with DNA encompassing the high affinity purF operator site and which is 16 base-pairs long with 5'-deoxynucleoside overhangs on each complementary strand. The crystals diffract to better than 2.6 A and take the orthorhombic space group C222(1), with unit cell dimensions a = 175.9 A, b = 94.8 A and c = 81.8 A. The structure determination of this PurR-hypoxanthine-DNA complex will provide the first high resolution view of a Lacl member-DNA complex. |
| Links |
PubMed Online version:10.1006/jmbi.1994.1580 |
| Keywords |
Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Base Sequence; Crystallization; Crystallography, X-Ray; DNA, Bacterial/chemistry; DNA, Bacterial/genetics; DNA, Bacterial/metabolism; Escherichia coli/chemistry; Escherichia coli Proteins; Hypoxanthine; Hypoxanthines/chemistry; Hypoxanthines/metabolism; Molecular Sequence Data; Molecular Structure; Operator Regions, Genetic/genetics; Repressor Proteins/chemistry; Repressor Proteins/metabolism |
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