X-ray crystallographic analysis of pokeweed antiviral protein-II after reductive methylation of lysine residues

Biochem Biophys Res Commun. 2000 Aug 28;275(2):549-52. doi: 10.1006/bbrc.2000.3329.

Abstract

Pokeweed antiviral protein II (PAP-II) is a naturally occurring protein isolated from early summer leaves of the pokeweed plant (Phytolacca americana). PAP-II belongs to a family of ribosome-inactivating proteins which catalytically deadenylate ribosomal and viral RNA. The chemical modification of PAP-II by reductive methylation of its lysine residues significantly improved the crystal quality for X-ray diffraction studies. Hexagonal crystals of the modified PAP-II, with unit cell parameters a = b = 92.51 A, c = 79.05 A, were obtained using 1.8 M Na/K phosphate as the precipitant. These crystals contained one enzyme molecule per asymmetric unit and diffracted up to 2.4 A, when exposed to a synchroton source.

Publication types

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

MeSH terms

  • Crystallography, X-Ray
  • Lysine / metabolism*
  • Methylation
  • N-Glycosyl Hydrolases*
  • Plant Proteins / chemistry*
  • Plant Proteins / metabolism
  • Protein Conformation
  • Ribosome Inactivating Proteins, Type 1

Substances

  • Plant Proteins
  • Ribosome Inactivating Proteins, Type 1
  • N-Glycosyl Hydrolases
  • pokeweed antiviral protein
  • Lysine