Highly Ordered Protein Nanorings Designed by Accurate Control of Glutathione S‑Transferase Self-Assembly
- Publication date
- 2013
- Publisher
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 <i>C</i><sub>2</sub>-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