Structure and assembly of scalable porous protein cages
| Autor: | Sasaki, Eita, Böhringer, Daniel, van de Waterbeemd, Michiel, Leibundgut, Marc, Zschoche, Reinhard, Heck, Albert J R, Ban, Nenad, Hilvert, Donald, Biomolecular Mass Spectrometry and Proteomics, Sub Biomol.Mass Spectrometry & Proteom., Afd Biomol.Mass Spect. and Proteomics |
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| Přispěvatelé: | Biomolecular Mass Spectrometry and Proteomics, Sub Biomol.Mass Spectrometry & Proteom., Afd Biomol.Mass Spect. and Proteomics |
| Rok vydání: | 2017 |
| Předmět: |
Protein Conformation
alpha-Helical 0301 basic medicine Materials science Science Static Electricity Protein design Beta sheet Gene Expression General Physics and Astronomy Nanotechnology Protein Engineering 010402 general chemistry 01 natural sciences Article General Biochemistry Genetics and Molecular Biology Lumazine synthase 03 medical and health sciences Dodecahedron Protein structure Bacterial Proteins Multienzyme Complexes Cryoelectron microscopy Static electricity Escherichia coli Molecular self-assembly Protein Interaction Domains and Motifs Cloning Molecular Drug Carriers Multidisciplinary Bacteria Mass spectrometry biology General Chemistry Protein engineering Recombinant Proteins 0104 chemical sciences Protein Subunits 030104 developmental biology Chemical engineering biology.protein Molecular evolution Protein Conformation beta-Strand Protein Multimerization Porosity |
| Zdroj: | Nature Communications Nature Communications, 8. Nature Publishing Group Nature Communications, Vol 8, Iss 1, Pp 1-10 (2017) Nature Communications, 8 |
| ISSN: | 2041-1723 |
| Popis: | Proteins that self-assemble into regular shell-like polyhedra are useful, both in nature and in the laboratory, as molecular containers. Here we describe cryo-electron microscopy (EM) structures of two versatile encapsulation systems that exploit engineered electrostatic interactions for cargo loading. We show that increasing the number of negative charges on the lumenal surface of lumazine synthase, a protein that naturally assembles into a ∼1-MDa dodecahedron composed of 12 pentamers, induces stepwise expansion of the native protein shell, giving rise to thermostable ∼3-MDa and ∼6-MDa assemblies containing 180 and 360 subunits, respectively. Remarkably, these expanded particles assume unprecedented tetrahedrally and icosahedrally symmetric structures constructed entirely from pentameric units. Large keyhole-shaped pores in the shell, not present in the wild-type capsid, enable diffusion-limited encapsulation of complementarily charged guests. The structures of these supercharged assemblies demonstrate how programmed electrostatic effects can be effectively harnessed to tailor the architecture and properties of protein cages. Nature Communications, 8 ISSN:2041-1723 |
| Databáze: | OpenAIRE |
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