Crystallization and preliminary X-ray crystallographic analysis of human quinolinate phosphoribosyltransferase

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Jan 1;67(Pt 1):38-40. doi: 10.1107/S1744309110041011. Epub 2010 Dec 21.

Abstract

Quinolinate phosphoribosyltransferase (QPRTase) is a key NAD-biosynthetic enzyme which catalyzes the transfer of quinolinic acid to 5-phosphoribosyl-1-pyrophosphate, yielding nicotinic acid mononucleotide. Homo sapiens QPRTase (Hs-QPRTase) appeared as a hexamer during purification and the protein was crystallized. Diffraction data were collected and processed at 2.8 Å resolution. Native Hs-QPRTase crystals belonged to space group P2(1), with unit-cell parameters a=76.2, b=137.1, c=92.7 Å, β=103.8°. Assuming the presence of six molecules in the asymmetric unit, the calculated Matthews coefficient is 2.46 Å3 Da(-1), which corresponds to a solvent content of 49.9%.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Crystallization
  • Crystallography, X-Ray
  • Humans
  • Molecular Sequence Data
  • NAD / biosynthesis
  • Pentosyltransferases / chemistry*
  • Pentosyltransferases / metabolism
  • Protein Structure, Quaternary*

Substances

  • NAD
  • Pentosyltransferases
  • nicotinate-nucleotide diphosphorylase (carboxylating)