Preliminary crystallographic characterization of ricin agglutinin

Proteins. 1997 Aug;28(4):586-9. doi: 10.1002/(sici)1097-0134(199708)28:4<586::aid-prot12>3.0.co;2-c.

Abstract

The quaternary structure of ricin agglutinin (RCA) has been determined by x-ray crystallography. The refined structure of ricin proved to be a successful search model using the molecular replacement method of phase determination. RCA forms an elongated molecule of dimensions 120 A x 60 A x 40 A with two A chains at the center and a B chain at each end. The A chains are covalently associated via a disulfide bridge between Cys 156 of both chains. Additional contacts at residues 114-5 stabilize the dimer interface. The covalent association of RCAA chains was confirmed by gel filtration under reducing and nonreducing conditions.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallography, X-Ray
  • Lectins / chemistry*
  • Models, Molecular
  • Plant Lectins*
  • Protein Conformation*

Substances

  • Lectins
  • Plant Lectins
  • Ricinus communis agglutinin-1