Interaction between a Type-II Dockerin Domain and a Type-II Cohesin Domain from Clostridium thermocellum Cellulosome

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  • Interaction between a Type-2 Dockerin Domain and a Type-2 Cohesin Domain from Clostridium thermocellum Cellulosome
  • Interaction between a Type-II Dockerin Domain and a Type-II Cohesin Domain from<i>Clostridium thermocellum</i>Cellulosome

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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 (KD) value was 1.8×10−9 M, which is a little larger than that for the combination of a type-I dockerin and a type-I cohesin.

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