Highly Ordered Protein Nanorings Designed by Accurate Control of Glutathione S-Transferase Self-Assembly

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• 作者：Yushi Bai ; Quan Luo ; Wei Zhang ; Lu Miao ; Jiayun Xu ; Hongbin Li ; Junqiu Liu
• 刊名：The Journal of the American Chemical Society
• 出版年：2013
• 出版时间：July 31, 2013
• 年：2013
• 卷：135
• 期：30
• 页码：10966-10969
• 全文大小：352K
• 年卷期：v.135,no.30(July 31, 2013)
• ISSN：1520-5126

文摘

Protein self-assembly into exquisite, complex, yet highly ordered architectures represents the supreme wisdom of nature. However, precise manipulation of protein self-assembly behavior in vitro is a great challenge. Here we report that by taking advantage of the cooperation of metal-ion-chelating interactions and nonspecific protein鈥損rotein interactions, we achieved accurate control of the orientation of proteins and their self-assembly into protein nanorings. As a building block, we utilized the C₂-symmetric protein sjGST-2His, a variant of glutathione S-transferase from Schistosoma japonicum having two properly oriented His metal-chelating sites on the surface. Through synergic metal-coordination and non-covalent interactions, sjGST-2His self-assembled in a fixed bending manner to form highly ordered protein nanorings. The diameters of the nanorings can be regulated by tuning the strength of the non-covalent interaction network between sjGST-2His interfaces through variation of the ionic strength of the solution. This work provides a de novo design strategy that can be applied in the construction of novel protein superstructures.