8P4Y

Coiled-coil protein origami triangle

8P4Y の概要

• エントリーDOI: 10.2210/pdb8p4y/pdb
• 分子名称: Protein origami triangle, GLYCEROL (3 entities in total)
• 機能のキーワード: coiled-coil, protein origami, designed protein, de novo protein
• 由来する生物種: synthetic construct
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24496.32

構造登録者

Satler, T.,Hadzi, S.,Jerala, R. (登録日: 2023-05-23, 公開日: 2023-08-02, 最終更新日: 2023-08-23)

主引用文献

Satler, T.,Hadzi, S.,Jerala, R.
Crystal Structure of de Novo Designed Coiled-Coil Protein Origami Triangle.
J.Am.Chem.Soc., 145:16995-17000, 2023

PubMed Abstract: Coiled-coil protein origami (CCPO) uses modular coiled-coil building blocks and topological principles to design polyhedral structures distinct from those of natural globular proteins. While the CCPO strategy has proven successful in designing diverse protein topologies, no high-resolution structural information has been available about these novel protein folds. Here we report the crystal structure of a single-chain CCPO in the shape of a triangle. While neither cyclization nor the addition of nanobodies enabled crystallization, it was ultimately facilitated by the inclusion of a GCN homodimer. Triangle edges are formed by the orthogonal parallel coiled-coil dimers P1:P2, P3:P4, and GCN connected by short linkers. A triangle has a large central cavity and is additionally stabilized by side-chain interactions between neighboring segments at each vertex. The crystal lattice is densely packed and stabilized by a large number of contacts between triangles. Interestingly, the polypeptide chain folds into a trefoil-type protein knot topology, and AlphaFold2 fails to predict the correct fold. The structure validates the modular CC-based protein design strategy, providing molecular insight underlying CCPO stabilization and new opportunities for the design.

PubMed: 37486611
DOI: 10.1021/jacs.3c05531

実験手法

X-RAY DIFFRACTION (2.052 Å)