The three-dimensional structure of the seed storage protein phaseolin at 3 A resolution

EMBO J. 1990 Jan;9(1):9-15.

Abstract

The polypeptides of the trimeric seed storage protein phaseolin comprise two structurally similar units each made up of a beta-barrel and an alpha-helical domain. The beta-barrel has the 'jelly-roll' folding topology of the viral coat proteins and the alpha-helical domain shows structural similarity to the helix-turn-helix motif found in certain DNA-binding proteins.

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Crystallization
  • Glycosylation
  • Macromolecular Substances
  • Molecular Sequence Data
  • Molecular Structure
  • Plant Proteins*
  • Protein Conformation
  • X-Ray Diffraction

Substances

  • Macromolecular Substances
  • Plant Proteins
  • phaseolin protein, Phaseolus vulgaris