五聚体
自组装
生物物理学
十二面体
静电
纳米技术
超嗜热菌
化学
结构生物学
结晶学
二十面体对称
蛋白质亚单位
蛋白质结构
类病毒颗粒
材料科学
生物
生物化学
基因
电气工程
工程类
大肠杆菌
重组DNA
作者
Eita Sasaki,Donald Hilvert
出处
期刊:Journal of the Pharmaceutical Society of Japan
日期:2019-01-31
卷期号:139 (2): 199-208
被引量:2
标识
DOI:10.1248/yakushi.18-00169-2
摘要
Proteins are excellent materials for constructing nano- to micro-meter sized compartments. For example, in nature, hollow spherical shells made of proteins, called protein cages, are widespread. Prominent examples include viruses, ferritins, carboxysomes, and others. Protein cages designed and engineered in the laboratory have also gained recent attention because of their potential use in synthetic biology, materials science, and medicine. Here, we show that engineered variants of lumazine synthase (LS) from Aquifex aeolicus self-assemble into porous shell-like structures, with striking size-expansion from the original dodecahedron composed of 12 pentamer subunits. Cryo-electron microscopy (EM) analysis has revealed that pentamers are the basic assembly units, although small conformational changes in each subunit lead to final expanded architectures composed of 36 and 72 pentamers. The underlying conformational changes likely arise from electrostatic repulsion between anionic residues originally introduced at the lumenal surface of the LS cage to encapsulate positively charged guest molecules. The plastic nature of the LS cage structure was also explored using a positively supercharged variant of the green fluorescent protein GFP(+36) as an assembly mediator. By controlling the favorable electrostatic interactions between the negatively charged LS cage and the positively charged mediator, multishell structures were created, as previously observed in some virus-like particles. These results highlight the potential of engineered LS cages for various future applications, including drug delivery and bioimaging.
科研通智能强力驱动
Strongly Powered by AbleSci AI