Crystallization and preliminary X-ray diffraction analysis of spermidine synthase from Helicobacter pylori.
Polyamines, such as putrescine, spermidine and spermine, are essential for the regulation of cell proliferation and differentiation in most organisms. Spermidine synthase catalyzes the transfer of the aminopropyl group from decarboxylated S-adenosylmethionine to putrescine in the biosynthesis of spermidine. In this study, spermidine synthase of Helicobacter pylori has been overexpressed in Escherichia coli and purified. Two kinds of spermidine synthase crystals were obtained. One belongs to the monoclinic P2(1) space group, with unit-cell parameters a = 62.78, b = 58.24, c = 74.28 A, beta = 90.9 degrees , and the other belongs to the orthorhombic C222(1) space group, with unit-cell parameters a = 100.43, b = 128.55, c = 143.60 A.
Lu
P K
PK
Institute of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu 300, Taiwan.
Chien
S Y
SY
Tsai
J Y
JY
Fong
C T
CT
Lee
M J
MJ
Huang
H
H
Sun
Y J
YJ
D003460:Crystallization; D018360:Crystallography, X-Ray; D016480:Helicobacter pylori / Q000201:enzymology*; D011436:Spermidine Synthase / Q000737:chemistry*
D011436:Spermidine Synthase