Crystallization and preliminary X-ray diffraction analysis of the glucuronoyl esterase catalytic domain from Hypocrea jecorina

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Apr 1;64(Pt 4):255-7. doi: 10.1107/S1744309108004594. Epub 2008 Mar 21.

Abstract

The catalytic domain of the glucuronoyl esterase from Hypocrea jecorina (anamorph Trichoderma reesei) was overexpresssed, purified and crystallized by the sitting-drop vapor-diffusion method using 1.4 M sodium/potassium phosphate pH 6.9. The crystals belonged to space group P2(1)2(1)2(1) and X-ray diffraction data were collected to 1.9 A resolution. This is the first enzyme with glucoronoyl esterase activity to be crystallized; its structure will be valuable in lignocellulose-degradation research.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Catalytic Domain* / genetics
  • Crystallization
  • Esterases / chemistry*
  • Esterases / metabolism
  • Fungal Proteins / chemistry*
  • Fungal Proteins / metabolism
  • Glucuronates / chemistry*
  • Glucuronates / metabolism
  • Hypocrea / enzymology*
  • Recombinant Proteins / chemistry
  • Substrate Specificity
  • Trichoderma / enzymology
  • X-Ray Diffraction

Substances

  • Fungal Proteins
  • Glucuronates
  • Recombinant Proteins
  • Esterases