Crystallization and preliminary X-ray analysis of CTP:phosphoethanolamine cytidylyltransferase (ECT) from Saccharomyces cerevisiae.
CTP:phosphoethanolamine cytidylyltransferase (ECT) is the enzyme that catalyzes the conversion of phosphoethanolamine to CDP-ethanolamine in the phosphatidylethanolamine-biosynthetic pathway (Kennedy pathway). ECT from Saccharomyces cerevisiae was crystallized by the sitting-drop vapour-diffusion method using PEG 4000 as precipitant. The crystals diffracted X-rays from a synchrotron-radiation source to 1.88 A resolution. The space group was assigned as primitive tetragonal, P4(1)2(1)2 or P4(3)2(1)2, with unit-cell parameters a = b = 66.3, c = 150.8 A. The crystals contain one ECT molecule in the asymmetric unit (V(M) = 2.2 A(3) Da(-1)), with a solvent content of 43%.
Ohtsuka
Jun
J
Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Bunkyo-ku, Tokyo 113-8657, Japan.
Nagata
Koji
K
Lee
Woo Cheol
WC
Ono
Yusuke
Y
Fukuda
Ryouichi
R
Ohta
Akinori
A
Tanokura
Masaru
M
D003460:Crystallization; D018360:Crystallography, X-Ray; D012316:RNA Nucleotidyltransferases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D012441:Saccharomyces cerevisiae / Q000201:enzymology*
D011994:Recombinant Proteins; D012316:RNA Nucleotidyltransferases; C504174:ECT1 protein, S cerevisiae; C020126:Ethanolamine-phosphate cytidylyltransferase