4NWR
Computationally Designed Two-Component Self-Assembling Tetrahedral Cage T33-28
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Summary for 4NWR
| Entry DOI | 10.2210/pdb4nwr/pdb |
| Related | 4NWN 4NWO 4NWP 4NWQ |
| Descriptor | integron gene cassette protein, Macrophage migration inhibitory factor-like protein (2 entities in total) |
| Functional Keywords | two-component, self-assembling, tetrahedron, designed protein cage, computational design, computational biology, protein engineering, multimerization, nanomaterial, nanostructure, integrons, macrophage migration-inhibitory factors, protein binding |
| Biological source | uncultured bacterium More |
| Total number of polymer chains | 96 |
| Total formula weight | 1502719.44 |
| Authors | McNamara, D.E.,King, N.P.,Bale, J.B.,Sheffler, W.,Baker, D.,Yeates, T.O. (deposition date: 2013-12-06, release date: 2014-05-28, Last modification date: 2023-09-20) |
| Primary citation | King, N.P.,Bale, J.B.,Sheffler, W.,McNamara, D.E.,Gonen, S.,Gonen, T.,Yeates, T.O.,Baker, D. Accurate design of co-assembling multi-component protein nanomaterials. Nature, 510:103-108, 2014 Cited by PubMed Abstract: The self-assembly of proteins into highly ordered nanoscale architectures is a hallmark of biological systems. The sophisticated functions of these molecular machines have inspired the development of methods to engineer self-assembling protein nanostructures; however, the design of multi-component protein nanomaterials with high accuracy remains an outstanding challenge. Here we report a computational method for designing protein nanomaterials in which multiple copies of two distinct subunits co-assemble into a specific architecture. We use the method to design five 24-subunit cage-like protein nanomaterials in two distinct symmetric architectures and experimentally demonstrate that their structures are in close agreement with the computational design models. The accuracy of the method and the number and variety of two-component materials that it makes accessible suggest a route to the construction of functional protein nanomaterials tailored to specific applications. PubMed: 24870237DOI: 10.1038/nature13404 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.5 Å) |
Structure validation
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