Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/50357
標題: Functional analysis of conserved aromatic amino acids in the discoidin domain of Paenibacillus beta-1,3-glucanase
作者: Cheng, Y.M.
孟孟孝
Hsieh, F.C.
Meng, M.S.
關鍵字: carbohydrate-binding module
clostridium-perfringens
bacterial
sialidase
cellulomonas-fimi
crystal-structure
genome sequence
c2
domain
factor-v
cloning
identification
期刊/報告no:: Microbial Cell Factories, Volume 8.
摘要: The 190-kDa Paenibacillus beta-1,3-glucanase (LamA) contains a catalytic module of the glycoside hydrolase family 16 (GH16) and several auxiliary domains. Of these, a discoidin domain (DS domain), present in both eukaryotic and prokaryotic proteins with a wide variety of functions, exists at the carboxyl-terminus. To better understand the bacterial DS domain in terms of its structure and function, this domain alone was expressed in Escherichia coli and characterized. The results indicate that the DS domain binds various polysaccharides and enhances the biological activity of the GH16 module on composite substrates. We also investigated the importance of several conserved aromatic residues in the domain's stability and substrate-binding affinity. Both were affected by mutations of these residues; however, the effect on protein stability was more notable. In particular, the forces contributed by a sandwiched triad (W1688, R1756, and W1729) were critical for the presumable beta-sandwich fold.
URI: http://hdl.handle.net/11455/50357
ISSN: 1475-2859
文章連結: http://dx.doi.org/10.1186/1475-2859-8-62
Appears in Collections:生物科技學研究所

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