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

TitleHighly Ordered Protein Nanorings Designed by Accurate Control of Glutathione S-Transferase Self-Assembly
Publication TypeJournal Article
Year of Publication2013
AuthorsBai, Y, Luo, Q, Zhang, W, Miao, L, Xu, J, Li, H, Liu, J
JournalJOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume135
Pagination10966-10969
Date PublishedJUL 31
ISSN0002-7863
Abstract

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 protein interactions, we achieved accurate control of the orientation of proteins and their self-assembly into protein nanorings. As a building block, we utilized the C-2-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.

DOI10.1021/ja405519s