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Title
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Crystallization and preliminary crystallographic investigation of glycosomal pyruvate phosphate dikinase from Trypanosoma brucei.
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Authors
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L.W.Cosenza,
F.Bringaud,
T.Baltz,
F.M.Vellieux.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2000,
56,
1688-1690.
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PubMed id
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Abstract
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The PP(i)-dependent glycosomal enzyme pyruvate phosphate dikinase (PPDK) from
Trypanosoma brucei is expressed in the insect stage of the parasite. Its precise
function there is still unclear, but the enzyme may catalyze the 'reverse
reaction' of transfer of phosphate from phosphoenolpyruvate (PEP) to generate
pyruvate as a means of scavenging large amounts of pyrophosphate. This protein
may represent a target for drug design against diseases caused by trypanosomes
and related kinetoplastids. The recombinant protein is 918 amino acids long
(predicted molecular mass approximately 100 kDa and pI = 8.9). Crystallization
conditions for the recombinant PPDK are reported that result in crystals that
diffract X-rays to better than 3.0 A resolution. Their space group is
P2(1)2(1)2, with unit-cell parameters a = 121.17, b = 153.5, c = 65.46 A, alpha
= beta = gamma = 90 degrees. The crystals, like the protein in solution, are
sensitive to temperature and fail to diffract or diffract only to low resolution
after ageing for two weeks or longer.
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