Crystallization and preliminary X-ray crystallographic analysis of UDP-glucuronic acid:flavonol-3-O-glucuronosyltransferase (VvGT5) from the grapevine Vitis vinifera

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Jan 1;69(Pt 1):65-8. doi: 10.1107/S1744309112045095. Epub 2012 Dec 25.

Abstract

Grapevine (Vitis vinifera) glycosyltransferase 5 (VvGT5) is a UDP-glucuronic acid:flavonol-3-O-glucuronosyltransferase that catalyses the 3-O-specific glucuronosylation of flavonols using UDP-glucuronic acid as a sugar donor to produce flavonol 3-O-glucosides, which are important bioactive phytochemicals. Recombinant VvGT5 expressed in Escherichia coli cells was purified and crystallized by the sitting-drop vapour-diffusion method. A full set of X-ray diffraction data was collected to 2.2 Å Bragg spacing from a single crystal using a synchrotron-radiation source. The crystal was hexagonal, belonging to space group P6(1)22, with unit-cell parameters a = b = 102.70, c = 535.92 Å. The initial phases were determined by the molecular-replacement method.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallization / methods
  • Crystallography, X-Ray
  • Escherichia coli / genetics
  • Glucosyltransferases / chemistry*
  • Glucosyltransferases / genetics
  • Glucosyltransferases / isolation & purification
  • Plant Proteins / chemistry*
  • Plant Proteins / genetics
  • Plant Proteins / isolation & purification
  • Protein Conformation
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Recombinant Proteins / isolation & purification
  • Vitis / enzymology*

Substances

  • Plant Proteins
  • Recombinant Proteins
  • Glucosyltransferases
  • flavonol 3-O-glucosyltransferase