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4NWO

Computationally Designed Two-Component Self-Assembling Tetrahedral Cage T33-15

Summary for 4NWO
Entry DOI10.2210/pdb4nwo/pdb
Related4NWN 4NWP 4NWQ 4NWR
DescriptorMolybdenum cofactor biosynthesis protein MogA, Chorismate mutase AroH, CALCIUM ION, ... (4 entities in total)
Functional Keywordstwo-component, self-assembling, tetrahedron, designed protein cage, computational design, protein engineering, multimerization, nanomaterial, nanostructure, molybdenum cofactor biosynthesis protein, mog, chorismate mutase, isomerase, protein binding
Biological sourceShewanella oneidensis
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Cellular locationCytoplasm (Potential): Q84FH6
Total number of polymer chains2
Total formula weight33603.80
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 citationKing, 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: 24870237
DOI: 10.1038/nature13404
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.8 Å)
Structure validation

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