Crystallization and preliminary x-ray structure determination of Lupinus luteus PR10 protein

Acta Crystallogr D Biol Crystallogr. 1999 Nov;55(Pt 11):1925-7. doi: 10.1107/s0907444999011221.

Abstract

The pathogenesis-related protein of the PR10 class from Lupinus luteus (yellow lupin), LlPR10.1A, is constitutively expressed in roots. It is also accumulated in leaves treated with a suspension of pathogenic bacteria as a response to stress. Recombinant yellow-lupin LlPR10.1A protein has been overexpressed in Escherichia coli as a fusion product with maltose-binding protein. LlPR10.1A crystallizes in the orthorhombic P2(1)2(1)2(1) space group and the crystals diffract to 2.45 A resolution. The structure has been solved by molecular replacement, using the structure of a birch-pollen allergen protein as a model.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • ATP-Binding Cassette Transporters*
  • Allergens*
  • Antigens, Plant
  • Carrier Proteins / chemistry
  • Carrier Proteins / genetics
  • Crystallization
  • Crystallography, X-Ray
  • Escherichia coli
  • Escherichia coli Proteins*
  • Fabaceae
  • Maltose-Binding Proteins
  • Models, Molecular
  • Monosaccharide Transport Proteins*
  • Plant Proteins / chemistry*
  • Plant Proteins / genetics
  • Plants, Medicinal
  • Protein Folding
  • Recombinant Fusion Proteins / chemistry
  • Recombinant Fusion Proteins / genetics

Substances

  • ATP-Binding Cassette Transporters
  • Allergens
  • Antigens, Plant
  • Carrier Proteins
  • Escherichia coli Proteins
  • Maltose-Binding Proteins
  • Monosaccharide Transport Proteins
  • Plant Proteins
  • Recombinant Fusion Proteins
  • maltose transport system, E coli
  • pathogenesis-related proteins, plant
  • Bet v 1 allergen, Betula