Interaction between a Type-II Dockerin Domain and a Type-II Cohesin Domain from Clostridium thermocellum Cellulosome
Interaction between a Type-II Dockerin Domain and a Type-II Cohesin Domain from Clostridium thermocellum Cellulosome
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DOI：
10.1271/bbb.68.924
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发表时间：
2004-01
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影响因子：
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通讯作者：
Sadanari Jindou;T. Kajino;M. Inagaki;S. Karita;P. Béguin;Tetsuya Kimura;K. Sakka;K. Ohmiya
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文献类型：
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作者：
Sadanari Jindou;T. Kajino;M. Inagaki;S. Karita;P. Béguin;Tetsuya Kimura;K. Sakka;K. Ohmiya
支架蛋白CipA的II型锚定蛋白结构域与外层蛋白SdbA的II型粘着蛋白结构域之间的相互作用是将多纤维素酶体锚定到热纤梭菌细胞表面的基本机制。我们构建并纯化了一个dockerin多肽和一个cohesin多肽，并用表面等离子体共振方法测定了它们之间相互作用的亲和常数。解离常数（KD）值为1.8×10−9 M，略大于I型锚定蛋白和I型粘附蛋白的结合。
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 1.8×10−9 M, which is a little larger than that for the combination of a type-I dockerin and a type-I cohesin.