9DGH

Focused region on azoRhuA-bCDRhuA co-assembled nanotubes

これはPDB形式変換不可エントリーです。

9DGH の概要

• エントリーDOI: 10.2210/pdb9dgh/pdb
• EMDBエントリー: 46826
• 分子名称: 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)
• 機能のキーワード: assembly, lyase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 16
• 化学式量合計: 485384.87

構造登録者

Zhang, Z.,Sonani, R.R.,Wang, F.,Egelman, E.H.,Tezcan, F.A. (登録日: 2024-09-02, 公開日: 2025-07-16, 最終更新日: 2025-09-10)

主引用文献

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

実験手法

ELECTRON MICROSCOPY (3.03 Å)