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  • Crystallization and preliminary X-ray crystallographic study of 1-deoxy-D-xylulose 5-phosphate reductoisomerase from Plasmodium falciparum #MMPMID20208174
  • Umeda T; Tanaka N; Kusakabe Y; Nakanishi M; Kitade Y; Nakamura KT
  • Acta Crystallogr Sect F Struct Biol Cryst Commun 2010[Mar]; 66 (Pt 3): 330-2 PMID20208174garesp_yesshow ga
  • The nonmevalonate pathway of isoprenoid biosynthesis present in Plasmodium falciparum is known to be an effective target for antimalarial drugs. The second enzyme of the nonmevalonate pathway, 1-deoxy-D-xylulose 5-phosphate reductoisomerase (DXR), catalyzes the transformation of 1-deoxy-D-xylulose 5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP). For crystallographic studies, DXR from the human malaria parasite P. falciparum (PfDXR) was overproduced in Escherichia coli, purified and crystallized using the hanging-drop vapour-diffusion method in the presence of NADPH. X-ray diffraction data to 1.85 A resolution were collected from a monoclinic crystal form belonging to space group C2 with unit-cell parameters a = 168.89, b = 59.65, c = 86.58 A, beta = 117.8 degrees. Structural analysis by molecular replacement is in progress.
  • |Aldose-Ketose Isomerases/*chemistry/genetics/isolation & purification[MESH]
  • |Crystallization[MESH]
  • |Crystallography, X-Ray[MESH]
  • |Gene Expression[MESH]
  • |Multienzyme Complexes/*chemistry/genetics/isolation & purification[MESH]
  • |Oxidoreductases/*chemistry/genetics/isolation & purification[MESH]
  • |Plasmodium falciparum/*enzymology[MESH]

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  • garesp_yesshow ga

    330 Pt 3.66 2010