Molecular-replacement studies of Trichosanthes kirilowii lectin 1: a structure belonging to the family of type 2 ribosome-inactivating proteins

Acta Crystallogr D Biol Crystallogr. 2000 Aug;56(Pt 8):1073-5. doi: 10.1107/s0907444900008192.

Abstract

Trichosanthes kirilowii lectin 1 (TKL-1) isolated from the tuber of T. kirilowii consists of two chains, each with a molecular weight of about 30 kDa. It has immunological properties which are similar to some ribosome-inactivating proteins (RIPs). TKL-1 was crystallized in space group P2(1)2(1)2(1) and diffraction data were collected to 2.7 A resolution. The molecular-replacement method was applied to solve the structure, using different chains of ricin, abrin-a and trichosanthin as search models. A set of consistent solutions was further verified by R(omit) profile analysis. In addition, the spatial arrangement of the two chains of TKL-1 is identical to that of type 2 RIPs.

MeSH terms

  • Crystallization
  • Crystallography, X-Ray
  • Lectins / chemistry*
  • Lectins / isolation & purification
  • Models, Molecular
  • Molecular Weight
  • Plant Lectins
  • Plants, Medicinal / chemistry*
  • Protein Structure, Quaternary
  • Ribosomes

Substances

  • Lectins
  • Plant Lectins