Reprogramming an ATP-driven protein machine into a light-gated nanocage.

Area of Science:

• Biochemistry
• Nanotechnology
• Structural Biology

Background:

• Natural protein assemblies exhibit complex architectures and functions, inspiring the engineering of artificial protein structures.
• Previous efforts to create functional protein assemblies faced challenges in achieving both defined structures and controllable functions.

Purpose of the Study:

• To engineer protein assemblies that function as light-controlled nanocontainers.
• To demonstrate light-triggered conformational changes in protein assemblies for controllable cargo manipulation.

Main Methods:

• Engineering photoswitchable azobenzene molecules into an adenosine-5'-triphosphate-driven group II chaperonin.
• Utilizing different wavelengths of light to induce conformational changes.
• Visualizing assembly states using single-particle cryo-electron microscopy.

Main Results:

• Reprogrammed group II chaperonin to open and close in response to specific light wavelengths.
• Demonstrated light-induced conformational changes driven by azobenzene moiety.
• Successfully used engineered nanocages for capturing and releasing non-native cargos.

Conclusions:

• Protein assemblies can be engineered into functional, light-controlled nanocontainers.
• Photoswitchable molecules integrated into protein structures enable precise control over nanoscale machines.
• This strategy offers a pathway for developing novel controllable nanoscale devices.