Structure and Flexibility of Nanoscale Protein Cages Designed by Symmetric Self-Assembly
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- 作者：Yen-Ting Lai ; Kuang-Lei Tsai ; Michael R. Sawaya ; Francisco J. Asturias ; Todd O. Yeates
- 刊名：The Journal of the American Chemical Society
- 出版年：2013
- 出版时间：May 22, 2013
- 年：2013
- 卷：135
- 期：20
- 页码：7738-7743
- 全文大小：362K
- 年卷期：v.135,no.20(May 22, 2013)
- ISSN：1520-5126
文摘
Designing protein molecules that self-assemble into complex architectures is an outstanding goal in the area of nanobiotechnology. One design strategy for doing this involves genetically fusing together two natural proteins, each of which is known to form a simple oligomer on its own (e.g., a dimer or trimer). If two such components can be fused in a geometrically predefined configuration, that designed subunit can, in principle, assemble into highly symmetric architectures. Initial experiments showed that a 12-subunit tetrahedral cage, 16 nm in diameter, could be constructed following such a procedure [Padilla, J. E.; et al. Proc. Natl. Acad. Sci. U.S.A.2001, 98, 2217; Lai, Y. T.; et al. Science2012, 336, 1129]. Here we characterize multiple crystal structures of protein cages constructed in this way, including cages assembled from two mutant forms of the same basic protein subunit. The flexibilities of the designed assemblies and their deviations from the target model are described, along with implications for further design developments.