Purification, crystallization and preliminary crystallographic studies of the ligand-binding domain of a plant vacuolar sorting receptor

Acta Crystallogr D Biol Crystallogr. 2004 Nov;60(Pt 11):2028-30. doi: 10.1107/S0907444904021031. Epub 2004 Oct 20.

Abstract

Vacuolar sorting receptor (VSR) proteins bind soluble protein ligands in a sequence-specific manner and target them to the lytic vacuole in plant cells. A VSR from Arabidopsis thaliana, AtBP80b, has been successfully purified after heterologous expression in Drosophila S2 cells. The AtBP80b protein (560 amino acids) was crystallized by the hanging-drop method with a PEG 400-based precipitant. Preliminary X-ray diffraction studies of an AtBP80b crystal showed that it belongs to the cubic space group P2(1)3 (or P4(2)32) and has unit-cell parameters a = b = c = 145.9 A. Crystals of the VSR diffract beyond 2.5 A resolution.

Publication types

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

MeSH terms

  • Animals
  • Arabidopsis / chemistry*
  • Arabidopsis Proteins / chemistry*
  • Arabidopsis Proteins / genetics
  • Arabidopsis Proteins / isolation & purification
  • Arabidopsis Proteins / metabolism*
  • Binding Sites
  • Cell Line
  • Crystallization
  • Crystallography, X-Ray
  • Drosophila / genetics
  • Ligands
  • Protein Structure, Tertiary
  • Vesicular Transport Proteins / chemistry*
  • Vesicular Transport Proteins / genetics
  • Vesicular Transport Proteins / isolation & purification
  • Vesicular Transport Proteins / metabolism*

Substances

  • Arabidopsis Proteins
  • BP80b protein, Arabidopsis
  • Ligands
  • Vesicular Transport Proteins