4EGG: Computationally Designed Self-assembling tetrahedron protein, T310

Citation:
Abstract
We describe a general computational method for designing proteins that self-assemble to a desired symmetric architecture. Protein building blocks are docked together symmetrically to identify complementary packing arrangements, and low-energy protein-protein interfaces are then designed between the building blocks in order to drive self-assembly. We used trimeric protein building blocks to design a 24-subunit, 13-nm diameter complex with octahedral symmetry and a 12-subunit, 11-nm diameter complex with tetrahedral symmetry. The designed proteins assembled to the desired oligomeric states in solution, and the crystal structures of the complexes revealed that the resulting materials closely match the design models. The method can be used to design a wide variety of self-assembling protein nanomaterials.
PDB ID: 4EGGDownload
MMDB ID: 100151
PDB Deposition Date: 2012/3/30
Updated in MMDB: 2017/11
Experimental Method:
x-ray diffraction
Resolution: 2.21  Å
Source Organism:
Similar Structures:
Biological Unit for 4EGG: dodecameric; determined by author and by software (PISA)
Molecular Components in 4EGG
Label Count Molecule
Proteins (12 molecules)
12
Putative Acetyltransferase Sacol2570
Molecule annotation
Chemicals (16 molecules)
1
16
* Click molecule labels to explore molecular sequence information.

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