Resonance assignments of cohesin and dockerin domains from Clostridium acetobutylicum ATCC824

CORC > 青岛生物能源与过程研究所 > 中国科学院青岛生物能源与过程研究所 > 代谢物组学团队

	Resonance assignments of cohesin and dockerin domains from Clostridium acetobutylicum ATCC824
	Cui, Zhenling; Li, Yifei; Xiao, Yan; Feng, Yingang; Cui, Qui
刊名	BIOMOLECULAR NMR ASSIGNMENTS
	2013-04-01
卷号	7 期号:1 页码:73-76
关键词	Cohesin Dockerin Clostridium acetobutylicum Cellulosome NMR
中文摘要	Cohesin and dockerin domains are critical assembling components of cellulosome, a large extracellular multienzyme complex which is used by anaerobic cellulolytic bacteria to efficiently degrade lignocellulose. According to sequence homology, cohesins can be divided into three major groups, whereas cohesins from Clostridium acetobutylicum are beyond these groups and emanate from a branching point between the type I and type III cohesins. Cohesins and dockerins from C. acetobutylicum show low sequence homology to those from other cellulolytic bacteria, and their interactions are specific in corresponding species. Therefore the interactions between cohesins and dockerins from C. acetobutylicum are meaningful to the studies of both cellulosome assembling mechanism and the construction of designer cellulosome. Here we report the NMR resonance assignments of one cohesin from cellulosome scaffoldin cipA and one dockerin from a cellulosomal glycoside hydrolase (family 9) of C. acetobutylicum for further structural determination and functional studies.
英文摘要	Cohesin and dockerin domains are critical assembling components of cellulosome, a large extracellular multienzyme complex which is used by anaerobic cellulolytic bacteria to efficiently degrade lignocellulose. According to sequence homology, cohesins can be divided into three major groups, whereas cohesins from Clostridium acetobutylicum are beyond these groups and emanate from a branching point between the type I and type III cohesins. Cohesins and dockerins from C. acetobutylicum show low sequence homology to those from other cellulolytic bacteria, and their interactions are specific in corresponding species. Therefore the interactions between cohesins and dockerins from C. acetobutylicum are meaningful to the studies of both cellulosome assembling mechanism and the construction of designer cellulosome. Here we report the NMR resonance assignments of one cohesin from cellulosome scaffoldin cipA and one dockerin from a cellulosomal glycoside hydrolase (family 9) of C. acetobutylicum for further structural determination and functional studies.
学科主题	代谢物组学
WOS标题词	Science & Technology ; Life Sciences & Biomedicine ; Technology
类目[WOS]	Biophysics ; Spectroscopy
研究领域[WOS]	Biophysics ; Spectroscopy
关键词[WOS]	MINICELLULOSOME ; PROTEIN
收录类别	SCI
语种	英语
WOS记录号	WOS:000316126100018
公开日期	2012-11-11
内容类型	期刊论文
源URL	[http://ir.qibebt.ac.cn:8080/handle/337004/1224]
专题	青岛生物能源与过程研究所_代谢物组学团队
作者单位	Chinese Acad Sci, Qingdao Inst Bioenergy & Bioproc Technol, Qingdao 266101, Peoples R China
推荐引用方式 GB/T 7714	Cui, Zhenling,Li, Yifei,Xiao, Yan,et al. Resonance assignments of cohesin and dockerin domains from Clostridium acetobutylicum ATCC824[J]. BIOMOLECULAR NMR ASSIGNMENTS,2013,7(1):73-76.
APA	Cui, Zhenling,Li, Yifei,Xiao, Yan,Feng, Yingang,&Cui, Qui.(2013).Resonance assignments of cohesin and dockerin domains from Clostridium acetobutylicum ATCC824.BIOMOLECULAR NMR ASSIGNMENTS,7(1),73-76.
MLA	Cui, Zhenling,et al."Resonance assignments of cohesin and dockerin domains from Clostridium acetobutylicum ATCC824".BIOMOLECULAR NMR ASSIGNMENTS 7.1(2013):73-76.