Resonance assignments of cohesin and dockerin domains from Clostridium acetobutylicum ATCC824
文献类型：期刊论文
| 作者 | Cui, Zhenling; Li, Yifei; Xiao, Yan; Feng, Yingang; Cui, Qui |
| 刊名 | BIOMOLECULAR NMR ASSIGNMENTS
 |
| 出版日期 | 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. |
| WOS标题词 | Science & Technology ; Life Sciences & Biomedicine ; Technology |
| 学科主题 | 代谢物组学 |
| 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 |
| 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. |
入库方式： OAI收割
来源：青岛生物能源与过程研究所
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