4QCC

Structure of a cube-shaped, highly porous protein cage designed by fusing symmetric oligomeric domains

4QCC の概要

• エントリーDOI: 10.2210/pdb4qcc/pdb
• 分子名称: 2-dehydro-3-deoxy-6-phosphogalactonate aldolase, peptidyl-prolyl cis-trans isomerase chimera (1 entity in total)
• 機能のキーワード: protein design, bionanotechnology, self-assembly, symmetry, porous biomaterials, structural protein, lyase
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 62466.92

構造登録者

Lai, Y.-T.,Yeates, T.O. (登録日: 2014-05-10, 公開日: 2014-11-19, 最終更新日: 2024-02-28)

主引用文献

Lai, Y.T.,Reading, E.,Hura, G.L.,Tsai, K.L.,Laganowsky, A.,Asturias, F.J.,Tainer, J.A.,Robinson, C.V.,Yeates, T.O.
Structure of a designed protein cage that self-assembles into a highly porous cube.
Nat Chem, 6:1065-1071, 2014

PubMed Abstract: Natural proteins can be versatile building blocks for multimeric, self-assembling structures. Yet, creating protein-based assemblies with specific geometries and chemical properties remains challenging. Highly porous materials represent particularly interesting targets for designed assembly. Here, we utilize a strategy of fusing two natural protein oligomers using a continuous alpha-helical linker to design a novel protein that self assembles into a 750 kDa, 225 Å diameter, cube-shaped cage with large openings into a 130 Å diameter inner cavity. A crystal structure of the cage showed atomic-level agreement with the designed model, while electron microscopy, native mass spectrometry and small angle X-ray scattering revealed alternative assembly forms in solution. These studies show that accurate design of large porous assemblies with specific shapes is feasible, while further specificity improvements will probably require limiting flexibility to select against alternative forms. These results provide a foundation for the design of advanced materials with applications in bionanotechnology, nanomedicine and material sciences.

PubMed: 25411884
DOI: 10.1038/nchem.2107

実験手法

X-RAY DIFFRACTION (7.078 Å)