Structural highlights
Publication Abstract from PubMedThe self-assembly of proteins into higher order structures is ubiquitous in living systems. It is also an essential process for the bottom-up creation of novel molecular architectures and devices for synthetic biology. However, the complexity of protein-protein interaction surfaces makes it challenging to mimic natural assembly processes in artificial systems. Indeed, many successful computationally designed protein assemblies are pre-screened for 'designability', limiting the choice of components. Here, we report a simple and pragmatic strategy to assemble chosen multi-subunit proteins into more complex structures. A coiled-coil domain appended to one face of the pentameric cholera toxin B-subunit (CTB) enabled the ordered assembly of tubular supra-molecular complexes. X-ray crystallography and analysis of a tubular structure has revealed a hierarchical assembly process that displays features reminiscent of the polymorphic assembly of polyomavirus proteins. The approach provides a simple and straightforward method to direct the assembly of protein building blocks which present either termini on a single face of an oligomer. This scaffolding approach can be used to generate bespoke supramolecular assemblies of functional proteins. Additionally, structural resolution of the scaffolded assemblies highlight 'native-state' forced protein-protein interfaces, which may prove useful as starting conformations for future computational design. Directed assembly of homo-pentameric cholera toxin B-subunit proteins into higher-order structures using coiled-coil appendages.,Ross JF, Wildsmith GC, Johnson M, Hurdiss D, Hollingsworth K, Thompson RF, Mosayebi M, Trinh CH, Paci E, Pearson AR, Webb ME, Turnbull WB J Am Chem Soc. 2019 Mar 11. doi: 10.1021/jacs.8b11480. PMID:30856321[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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This page was last modified 07:56, 20 March 2019.