Interaction between a type-II dockerin domain and a type-II cohesin domain from Clostridium thermocellum cellulosome |
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Authors: | Jindou Sadanari Kajino Tsutomu Inagaki Minoru Karita Shuichi Beguin Pierre Kimura Tetsuya Sakka Kazuo Ohmiya Kunio |
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Affiliation: | Faculty of Bioresources, Mie University, Tsu, Japan. |
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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. |
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