Crystallization and preliminary diffraction studies of pentaerythritol tetranitrate reductase from Enterobacter cloacae PB2

Acta Crystallogr D Biol Crystallogr. 1998 Jul 1;54(Pt 4):675-7. doi: 10.1107/s0907444997017836.

Abstract

Pentaerythritol tetranitrate (PETN) reductase of Enterobacter cloacae PB2, a flavoprotein involved in the biodegradation of the explosive PETN, ethylene glycol dinitrate (EGDN) and glycerol trinitrate (GTN), was purified from an overexpressing strain of E. coli and crystallized at 293 K using the sitting-drop vapour-diffusion method. Diffraction data can be seen at 1.8 A. The primitive orthorhombic cell has a monomer in the asymmetric unit. Preliminary molecular-replacement calculations have been performed using a search model based on Old Yellow enzyme.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / isolation & purification
  • Crystallization
  • Crystallography, X-Ray
  • Enterobacter cloacae / enzymology*
  • NADPH Dehydrogenase / chemistry
  • Oxidoreductases / chemistry*
  • Oxidoreductases / isolation & purification
  • Protein Conformation

Substances

  • Bacterial Proteins
  • Oxidoreductases
  • NADPH Dehydrogenase
  • pentaerythritol tetranitrate reductase