Site-directed mutagenesis and expression of the soluble form of the family IIIa cellulose binding domain from the cellulosomal scaffolding protein of Clostridium cellulovorans

被引：15

作者：

Murashima, K ^{[1
]}

Kosugi, A ^{[1
]}

Doi, RH ^{[1
]}

机构：

[1] Univ Calif Davis, Sect Mol & Cellular Biol, Davis, CA 95616 USA

来源：

JOURNAL OF BACTERIOLOGY | 2005年 / 187卷 / 20期

关键词：

D O I：

10.1128/JB.187.20.7146-7149.2005

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

The planar and anchoring residues of the family IlIa cellulose binding domain (CBD) from the cellulosomal scaffolding protein of Clostridium cellulovorans were investigated by site-directed mutagenesis and cellulose binding studies. By fusion with maltose binding protein, the family IIIa recombinant wild-type and mutant CBDs from C. cellulovorans were expressed as soluble forms. Cellulose binding tests of the mutant CBDs indicated that the planar strip residues played a major role in cellulose binding and that the anchoring residues played only a minor role.

引用

页码：7146 / 7149

页数：4

共 45 条

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