9DGH

Focused region on azoRhuA-bCDRhuA co-assembled nanotubes

This is a non-PDB format compatible entry.

Summary for 9DGH

• Entry DOI: 10.2210/pdb9dgh/pdb
• EMDB information: 46826
• Descriptor: Rhamnulose-1-phosphate aldolase, Cyclic alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranuronic acid-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranuronic acid-(1-4)-alpha-D-glucopyranose, ZINC ION, ... (4 entities in total)
• Functional Keywords: assembly, lyase
• Biological source: Escherichia coli
• Total number of polymer chains: 16
• Total formula weight: 485384.87

Authors

Zhang, Z.,Sonani, R.R.,Wang, F.,Egelman, E.H.,Tezcan, F.A. (deposition date: 2024-09-02, release date: 2025-07-16, Last modification date: 2025-09-10)

Primary citation

Zhang, Z.,Chiang, H.T.,Xia, Y.,Avakyan, N.,Sonani, R.R.,Wang, F.,Egelman, E.H.,De Yoreo, J.J.,Pozzo, L.D.,Tezcan, F.A.
Design of light- and chemically responsive protein assemblies through host-guest interactions.
Chem, 11:-, 2025

PubMed Abstract: Host-guest interactions have been widely used to build responsive materials and molecular machines owing to their inherently dynamic nature, interaction specificity, and responsiveness to diverse stimuli. Here we have set out to exploit these advantages of host-guest chemistry in the design of dynamic protein assemblies, using a symmetric protein, RhuA, as a building block. We show that RhuA variant individually modified with β-cyclodextrin (βCD) (host) or azobenzene (guest) functionalities can specifically pair with each other to form highly ordered 1- and 2-D assemblies. Association and dissociation RhuA-RhuA assemblies can be controlled by UV and visible light as well as by small-molecule modulators of βCD-azobenzene interactions. Kinetics analyses reveal that RhuA-RhuA nanotubes assemble without a nucleation barrier, a highly unusual occurrence for helical supramolecular systems. Taken together, our findings provide a compelling example for achieving complex structural and dynamic outcomes in protein assembly through simple chemical design.

PubMed: 40862094
DOI: 10.1016/j.chempr.2024.102407

Experimental method

ELECTRON MICROSCOPY (3.03 Å)