| Literature DB >> 15118324 |
Sadanari Jindou1, Tsutomu Kajino, Minoru Inagaki, Shuichi Karita, Pierre Beguin, Tetsuya Kimura, Kazuo Sakka, Kunio Ohmiya.
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.Entities:
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Year: 2004 PMID: 15118324 DOI: 10.1271/bbb.68.924
Source DB: PubMed Journal: Biosci Biotechnol Biochem ISSN: 0916-8451 Impact factor: 2.043