PMID:11042088
| Citation |
Hamdan, S, Brown, SE, Thompson, PR, Yang, JY, Carr, PD, Ollis, DL, Otting, G and Dixon, NE (2000) Preliminary X-ray crystallographic and NMR studies on the exonuclease domain of the epsilon subunit of Escherichia coli DNA polymerase III. J. Struct. Biol. 131:164-9 |
|---|---|
| Abstract |
The structured core of the N-terminal 3'-5' exonuclease domain of epsilon, the proofreading subunit of Escherichia coli DNA polymerase III, was defined by multidimensional NMR experiments with uniformly (15)N-labeled protein: it comprises residues between Ile-4 and Gln-181. A 185-residue fragment, termed epsilon(1-185), was crystallized by the hanging drop vapor diffusion method in the presence of thymidine-5'-monophosphate, a product inhibitor, and Mn(2+) at pH 5.8. The crystals are tetragonal, with typical dimensions 0.2 mm x 0.2 mm x 1.0 mm, grow over about 2 weeks at 4 degrees C, and diffract X-rays to 2.0 A. The space group was determined to be P4(n)2(1)2 (n = 0, 1, 2, 3), with unit cell dimensions a = 60.8 A, c = 111.4 A. |
| Links |
PubMed Online version:10.1006/jsbi.2000.4291 |
| Keywords |
Catalytic Domain; Chymotrypsin/metabolism; Crystallization; Crystallography, X-Ray; DNA Polymerase III/chemistry; DNA Polymerase III/genetics; DNA Polymerase III/metabolism; Electrophoresis, Polyacrylamide Gel; Escherichia coli/enzymology; Exodeoxyribonucleases/chemistry; Exodeoxyribonucleases/genetics; Exodeoxyribonucleases/metabolism; Manganese/metabolism; Mutagenesis; Nuclear Magnetic Resonance, Biomolecular; Peptide Fragments/chemistry; Peptide Fragments/metabolism; Protein Structure, Tertiary; Protein Subunits; Sequence Alignment; Thymidine Monophosphate/metabolism |
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