Crystallization and preliminary X-ray analysis of CTP:phosphoethanolamine cytidylyltransferase (ECT) from Saccharomyces cerevisiae

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Oct 1;62(Pt 10):1003-5. doi: 10.1107/S1744309106035561. Epub 2006 Sep 30.

Abstract

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%.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallization
  • Crystallography, X-Ray
  • RNA Nucleotidyltransferases / chemistry*
  • RNA Nucleotidyltransferases / genetics
  • RNA Nucleotidyltransferases / isolation & purification
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Recombinant Proteins / isolation & purification
  • Saccharomyces cerevisiae / enzymology*

Substances

  • Recombinant Proteins
  • RNA Nucleotidyltransferases
  • ECT1 protein, S cerevisiae
  • Ethanolamine-phosphate cytidylyltransferase