Resonance assignments of cohesin and dockerin domains from Clostridium acetobutylicum ATCC824
Resonance assignments of cohesin and dockerin domains from Clostridium acetobutylicum ATCC824
复制标题
丙酮丁醇梭菌 ATCC824 的粘连蛋白和 dockerin 结构域的共振分配
DOI：
10.1007/s12104-012-9381-2
复制
发表时间：
2013-04-01
影响因子：
0.9
通讯作者：
Cui, Qui
中科院分区：
文献类型：
--
作者：
Cui, Zhenling;Li, Yifei;Cui, Qui
纤维素酶体是一种细胞外多酶复合体，厌氧纤维素分解菌利用其高效降解木质纤维素。根据序列同源性，粘着蛋白可分为三个主要组，而来自丙酮丁醇梭菌的粘着蛋白超出这些组，并且源自I型和III型粘着蛋白之间的分支点。C. acetobutylicum与其它纤维素分解菌的同源性较低，它们之间的相互作用在相应的物种中具有特异性。因此，C.丙酮丁醇对研究多纤维素酶体的组装机制和构建设计型多纤维素酶体具有重要意义。在这里，我们报告了一个来自多纤维体支架蛋白cipA的粘附蛋白和一个来自C. acetobutylicum进行进一步的结构测定和功能研究。
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.