Crystallization and preliminary X-ray diffraction studies of recombinant Escherichia coli 4-diphosphocytidyl-2-C-methyl-D-erythritol synthetase

Acta Crystallogr D Biol Crystallogr. 2001 Aug;57(Pt 8):1189-91. doi: 10.1107/s0907444901010137. Epub 2001 Jul 23.

Abstract

Diphosphocytidyl-methylerythritol (DPCME) synthetase is involved in the mevalonate-independent pathway of isoprenoid biosynthesis, where it catalyses the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from 2-C-methyl-D-erythritol 4-phosphate and CTP. The Escherichia coli enzyme has been cloned, expressed in high yield, purified and crystallized. Elongated tetragonal prismatic crystals grown by the hanging-drop vapour-diffusion method using polyethylene glycol (PEG) 4000 as the precipitant belong to space group P4(1)2(1)2 (or P4(3)2(1)2), with unit-cell parameters a = b = 73.60, c = 175.56 A. Diffraction data have been recorded to 2.4 A resolution using synchrotron radiation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cloning, Molecular
  • Crystallization
  • Crystallography, X-Ray
  • Escherichia coli / enzymology*
  • Nucleotidyltransferases / biosynthesis
  • Nucleotidyltransferases / chemistry*
  • Nucleotidyltransferases / genetics
  • Protein Conformation
  • Recombinant Proteins / chemistry

Substances

  • Recombinant Proteins
  • 4-diphosphocytidyl-2-C--methylerythritol synthase
  • Nucleotidyltransferases