4QCC
Structure of a cube-shaped, highly porous protein cage designed by fusing symmetric oligomeric domains
Summary for 4QCC
| Entry DOI | 10.2210/pdb4qcc/pdb |
| Descriptor | 2-dehydro-3-deoxy-6-phosphogalactonate aldolase, peptidyl-prolyl cis-trans isomerase chimera (1 entity in total) |
| Functional Keywords | protein design, bionanotechnology, self-assembly, symmetry, porous biomaterials, structural protein, lyase |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 2 |
| Total formula weight | 62466.92 |
| Authors | Lai, Y.-T.,Yeates, T.O. (deposition date: 2014-05-10, release date: 2014-11-19, Last modification date: 2024-02-28) |
| Primary citation | 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 Cited by 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: 25411884DOI: 10.1038/nchem.2107 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (7.078 Å) |
Structure validation
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