Protein self-assembly into exquisite, complicated yet high-ordered architectures represents the supreme wisdom of nature.However, precisely manipulating protein self-assembling behaviors in vitro is a great challenge.By taking advantage of the cooperation of metal chelating interactions, host-guest interaction and non-specific protein-protein interactions, accuracy control of the orientation of protein self-assembly has been achieved, and multi-enzyme active sites have been designed on these nanostructures[1-8].For example, we utilized a C2 symmetrical protein,glutathione S-transferase (sjGST-2His), with properly orientated metal chelating sites (2His) on the surface as building block.Under the synergic function of metal-coordination and non-specific protein-protein interactions, sjGST-2His self-assembled in a fixed bending way into highly-ordered protein nanorings.This work provides a de nove design strategy that can be applied in the construction of novel protein superstructures.