7XA4

Thermotoga maritima ferritin variant-Tm-E (S111H) with Zn

7XA4 の概要

• エントリーDOI: 10.2210/pdb7xa4/pdb
• 分子名称: Ferritin, ZINC ION (3 entities in total)
• 機能のキーワード: protein assembly, metal binding protein
• 由来する生物種: Thermotoga maritima
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17616.47

構造登録者

Liu, Y.,Zhao, G. (登録日: 2022-03-17, 公開日: 2023-02-15, 最終更新日: 2023-11-29)

主引用文献

Liu, Y.,Chen, X.,Yin, S.,Chang, X.,Lv, C.,Zang, J.,Leng, X.,Zhang, T.,Zhao, G.
Directed Self-Assembly of Dimeric Building Blocks into Networklike Protein Origami to Construct Hydrogels.
Acs Nano, 16:19472-19481, 2022

PubMed Abstract: Engineering proteins to construct self-assemblies is of crucial significance not only for understanding the sophisticated living systems but also for fabricating advanced materials with unexplored functions. However, due to the inherent chemical heterogeneity and structural complexity of the protein surface, designing complex protein assemblies in an anisotropic fashion remains challenging. Here, we describe a self-assembly approach to fabricating protein origami with a networklike structure by designing dual noncovalent interactions on the different positions of a single protein building block. With dimeric proteins as building blocks, 1D protein filaments were constructed by the designed metal coordination at key protein interfaces. Subsequently, the network superstructures were created by the cross-linking of the 1D protein filaments at branch point linkages through the second designed π-π stacking interactions. Notably, upon increasing the protein concentration, the formed protein networks convert into hydrogels with reversible, injectable, and self-healing properties, which have the ability to promote bone regeneration. This strategy could be used to fabricate other protein-based materials with unexplored functions.

PubMed: 36315654
DOI: 10.1021/acsnano.2c09391

実験手法

X-RAY DIFFRACTION (1.96 Å)