7XA2

Thermotoga maritima ferritin variant-Tm-E(S111H)

Summary for 7XA2

• Entry DOI: 10.2210/pdb7xa2/pdb
• Descriptor: Ferritin, FE (III) ION (3 entities in total)
• Functional Keywords: protein assembly, metal binding protein
• Biological source: Thermotoga maritima
• Total number of polymer chains: 1
• Total formula weight: 17541.50

Authors

Liu, Y.,Zhao, G. (deposition date: 2022-03-16, release date: 2023-02-15, Last modification date: 2023-11-29)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.84 Å)