Interaction between a type-II dockerin domain and a type-II cohesin domain from Clostridium thermocellum cellulosome

Biosci Biotechnol Biochem. 2004 Apr;68(4):924-6. doi: 10.1271/bbb.68.924.

Abstract

The interaction between the type-II dockerin domain of the scaffoldin protein CipA and the type-II cohesin domain of the outer layer protein SdbA is the fundamental mechanism for anchoring the cellulosome to the cell surface of Clostridium thermocellum. We constructed and purified a dockerin polypeptide and a cohesin polypeptide, and determined affinity constants of the interaction between them by the surface plasmon resonance method. The dissociation constant (K(D)) value was 1.8 x 10(-9) M, which is a little larger than that for the combination of a type-I dockerin and a type-I cohesin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Outer Membrane Proteins / chemistry
  • Bacterial Outer Membrane Proteins / metabolism
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism*
  • Cell Cycle Proteins
  • Cellulosomes / chemistry*
  • Cellulosomes / metabolism*
  • Chromosomal Proteins, Non-Histone
  • Clostridium / chemistry*
  • Clostridium / metabolism
  • Cohesins
  • Fungal Proteins
  • Membrane Proteins / chemistry
  • Membrane Proteins / metabolism
  • Nuclear Proteins / chemistry*
  • Protein Binding
  • Protein Structure, Tertiary
  • Surface Plasmon Resonance

Substances

  • Bacterial Outer Membrane Proteins
  • Bacterial Proteins
  • Cell Cycle Proteins
  • Chromosomal Proteins, Non-Histone
  • CipA protein, Clostridium
  • Fungal Proteins
  • Membrane Proteins
  • Nuclear Proteins
  • OlpB protein, Clostridium thermocellum
  • SdbA protein, bacteria