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Title
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Preliminary X-ray analysis of a truncated form of recombinant fructose-2,6-bisphosphatase.
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Authors
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Y.H.Lee,
K.Lin,
D.Okar,
N.L.Alfano,
R.Sarma,
J.W.Pflugrath,
S.J.Pilkis.
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Ref.
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J Mol Biol, 1994,
235,
1147-1151.
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PubMed id
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Abstract
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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 coli and
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 A, b = 43.5 A,
c = 57.6 A, alpha = 95.2 degrees, beta = 99.3 degrees, and gamma = 106.2
degrees. These crystals diffract to 2.0 A resolution when exposed to synchrotron
radiation and are suitable for crystallographic structure analysis.
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