Open AccessCrystallization and preliminary X‐ray crystallographic study of 1‐deoxy‐ d ‐xylulose 5‐phosphate reductoisomerase from Plasmodium falciparum
Author(s) -
Umeda Tomonobu,
Tanaka Nobutada,
Kusakabe Yoshio,
Nakanishi Masayuki,
Kitade Yukio,
Nakamura Kazuo T.
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110001739
Subject(s) - plasmodium falciparum , monoclinic crystal system , crystallization , chemistry , biosynthesis , escherichia coli , crystallography , stereochemistry , biochemistry , crystal structure , enzyme , biology , malaria , organic chemistry , gene , immunology
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 Å resolution were collected from a monoclinic crystal form belonging to space group C 2 with unit‐cell parameters a = 168.89, b = 59.65, c = 86.58 Å, β = 117.8°. Structural analysis by molecular replacement is in progress.