期刊
BIOTECHNOLOGY PROGRESS
卷 37, 期 5, 页码 -出版社
WILEY
DOI: 10.1002/btpr.3190
关键词
cellulosome; E2 nanocage; HBV; post translational ligation strategy; self-assembling protein nanocage; synthetic metabolon
资金
- National Science Foundation [DMR1609621, MCB1615731]
A new approach for protein co-localization using naturally occurring protein nanocages as a scaffold has been successfully demonstrated, showing the potential for in vivo enzyme cascading and applications. The simplicity of the assembly method makes it a promising strategy for various enzyme pathways.
The wide variety of enzymatic pathways that can benefit from enzyme scaffolding is astronomical. While enzyme co-localization based on protein, DNA, and RNA scaffolds has been reported, we still lack scaffolds that offer well-defined and uniform three-dimensional structures for enzyme organization. Here we reported a new approach for protein co-localization using naturally occurring protein nanocages as a scaffold. Two different nanocages, the 25 nm E2 and the 34 nm heptatitis B virus, were used to demonstrate the successfully co-localization of the endoglucanase CelA and cellulose binding domain using the robust SpyTag/SpyCatcher bioconjugation chemistry. Because of the simplicity of the assembly, this strategy is useful not only for in vivo enzyme cascading but also the potential for in vivo applications as well.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据