Purification, crystallization and preliminary X-ray crystallographic analysis of xylose reductase from Candida tropicalis

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Apr 1;65(Pt 4):419-21. doi: 10.1107/S1744309109008719. Epub 2009 Mar 26.

Abstract

Xylose reductase (XR), which requires NADPH as a co-substrate, catalyzes the reduction of D-xylose to xylitol, which is the first step in the metabolism of D-xylose. The detailed three-dimensional structure of XR will provide a better understanding of the biological significance of XR in the efficient production of xylitol from biomass. XR of molecular mass 36.6 kDa from Candida tropicalis was crystallized using the hanging-drop vapour-diffusion method. According to X-ray diffraction data from C. tropicalis XR crystals at 2.91 A resolution, the unit cell belongs to space group P3(1) or P3(2). Preliminary analysis indicated the presence of four XR molecules in the asymmetric unit, with 68.0% solvent content.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aldehyde Reductase / chemistry*
  • Aldehyde Reductase / isolation & purification*
  • Candida tropicalis / enzymology*
  • Crystallization
  • Crystallography, X-Ray
  • Electrophoresis, Polyacrylamide Gel

Substances

  • Aldehyde Reductase