| 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 |
| DOI | 10.1007/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. |
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