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

被引：21

作者：

Jindou, S

Kajino, T

Inagaki, M

Karita, S

Beguin, P

Kimura, T

Sakka, K

Ohmiya, K

机构：

[1] Mie Univ, Fac Bioresources, Tsu, Mie 5148507, Japan

[2] Toyota Cent Res & Dev Labs Inc, Special Res Lab 2, Nagakute, Aichi 4801192, Japan

[3] Inst Pasteur, Dept Biotechnol, F-75724 Paris 15, France

来源：

BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY | 2004年 / 68卷 / 04期

关键词：

Clostridium thermocellum; cellulosome; dockerin; cohesin; surface plasmon resonance;

D O I：

10.1271/bbb.68.924

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：924 / 926

页数：3

共 20 条

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[Anonymous], BIOTECHNOL BIOENG S

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