8J9M

Crystal Structure of Human H-Ferritin variant 123F assembling in solution3

8J9M の概要

• エントリーDOI: 10.2210/pdb8j9m/pdb
• 分子名称: Ferritin heavy chain, FE (III) ION (3 entities in total)
• 機能のキーワード: protein assembly, oxidoreductase
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 64309.99

構造登録者

Chen, X.,Zhao, G. (登録日: 2023-05-04, 公開日: 2024-01-31)

主引用文献

Chen, X.,Zhang, T.,Liu, H.,Zang, J.,Lv, C.,Du, M.,Zhao, G.
Shape-Anisotropic Assembly of Protein Nanocages with Identical Building Blocks by Designed Intermolecular pi-pi Interactions.
Adv Sci, 10:e2305398-e2305398, 2023

PubMed Abstract: Protein lattices that shift the structure and shape anisotropy in response to environmental cues are closely coupled to potential functionality. However, to design and construct shape-anisotropic protein arrays from the same building blocks in response to different external stimuli remains challenging. Here, by a combination of the multiple, symmetric interaction sites on the outer surface of protein nanocages and the tunable features of phenylalanine-phenylalanine interactions, a protein engineering approach is reported to construct a variety of superstructures with shape anisotropy, including 3D cubic, 2D hexagonal layered, and 1D rod-like crystalline protein nanocage arrays by using one single protein building block. Notably, the assembly of these crystalline protein arrays is reversible, which can be tuned by external stimuli (pH and ionic strength). The anisotropic morphologies of the fabricated macroscopic crystals can be correlated with the Å-to-nm scale protein arrangement details by crystallographic elucidation. These results enhance the understanding of the freedom offered by an object's symmetry and inter-object π-π stacking interactions for protein building blocks to assemble into direction- and shape-anisotropic biomaterials.

PubMed: 37870198
DOI: 10.1002/advs.202305398

実験手法

X-RAY DIFFRACTION (2.9 Å)