QIBEBT-IR  > 代谢物组学研究组
Resonance assignments of cohesin and dockerin domains from Clostridium acetobutylicum ATCC824
Cui, Zhenling; Li, Yifei; Xiao, Yan; Feng, Yingang; Cui, Qui
2013-04-01
发表期刊BIOMOLECULAR NMR ASSIGNMENTS
卷号7期号:1页码:73-76
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.; 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.
文章类型Article
关键词Cohesin Dockerin Clostridium Acetobutylicum Cellulosome Nmr
学科领域代谢物组学
WOS标题词Science & Technology ; Life Sciences & Biomedicine ; Technology
DOI10.1007/s12104-012-9381-2
关键词[WOS]MINICELLULOSOME ; PROTEIN
收录类别SCI
语种英语
WOS研究方向Biophysics ; Spectroscopy
WOS类目Biophysics ; Spectroscopy
WOS记录号WOS:000316126100018
引用统计
文献类型期刊论文
条目标识符http://ir.qibebt.ac.cn/handle/337004/1224
专题代谢物组学研究组
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.
条目包含的文件 下载所有文件
文件名称/大小 文献类型 版本类型 开放类型 使用许可
Resonance assignment(378KB) 开放获取使用许可浏览 下载
个性服务
推荐该条目
保存到收藏夹
查看访问统计
导出为Endnote文件
谷歌学术
谷歌学术中相似的文章
[Cui, Zhenling]的文章
[Li, Yifei]的文章
[Xiao, Yan]的文章
百度学术
百度学术中相似的文章
[Cui, Zhenling]的文章
[Li, Yifei]的文章
[Xiao, Yan]的文章
必应学术
必应学术中相似的文章
[Cui, Zhenling]的文章
[Li, Yifei]的文章
[Xiao, Yan]的文章
相关权益政策
暂无数据
收藏/分享
文件名: Resonance assignments of cohesin and dockerin domains from Clostridium acetobutylicum ATCC824..pdf
格式: Adobe PDF
所有评论 (0)
暂无评论
 

除非特别说明,本系统中所有内容都受版权保护,并保留所有权利。