| Autor: |
Lee, Yong-Hwan, Lin, Kai, Okar, David, Alfano, Nancy L., Sarma, Raghupathy, Pflugrath, James W., Pilkis, Simon J. |
| Zdroj: |
JMB Online (Journal of Molecular Biology); January 1994, Vol. 235 Issue: 3 p1147-1151, 5p |
| Abstrakt: |
The bisphosphatase domain of rat liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase and a C-terminal 30 amino acid truncated form were expressed in high yield in Escherichia coliand purified to homogeneity. The separately expressed bisphosphatase domain and its C-terminal truncated form had kinetic properties similar to the bisphosphatase of the intact bifunctional enzyme, but their turnover numbers were fourfold higher. The truncated enzyme crystallized in space group P1 with two molecules per asymmetric unit. The determined cell dimensions are: a= 41·9 Å, b= 43·5 Å, c= 57·6 Å, α = 95·2°, β = 99·3°, and γ = 106·2°. These crystals diffract to 2·0 Å resolution when exposed to synchrotron radiation and are suitable for crystallographic structure analysis. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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