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TitleAn ultra-stable gold-coordinated protein cage displaying reversible assembly.
Journal, issue, pagesNature, Vol. 569, Issue 7756, Page 438-442, Year 2019
Publish dateMay 8, 2019
AuthorsAli D Malay / Naoyuki Miyazaki / Artur Biela / Soumyananda Chakraborti / Karolina Majsterkiewicz / Izabela Stupka / Craig S Kaplan / Agnieszka Kowalczyk / Bernard M A G Piette / Georg K A Hochberg / Di Wu / Tomasz P Wrobel / Adam Fineberg / Manish S Kushwah / Mitja Kelemen / Primož Vavpetič / Primož Pelicon / Philipp Kukura / Justin L P Benesch / Kenji Iwasaki / Jonathan G Heddle /
PubMed AbstractSymmetrical protein cages have evolved to fulfil diverse roles in nature, including compartmentalization and cargo delivery, and have inspired synthetic biologists to create novel protein assemblies ...Symmetrical protein cages have evolved to fulfil diverse roles in nature, including compartmentalization and cargo delivery, and have inspired synthetic biologists to create novel protein assemblies via the precise manipulation of protein-protein interfaces. Despite the impressive array of protein cages produced in the laboratory, the design of inducible assemblies remains challenging. Here we demonstrate an ultra-stable artificial protein cage, the assembly and disassembly of which can be controlled by metal coordination at the protein-protein interfaces. The addition of a gold (I)-triphenylphosphine compound to a cysteine-substituted, 11-mer protein ring triggers supramolecular self-assembly, which generates monodisperse cage structures with masses greater than 2 MDa. The geometry of these structures is based on the Archimedean snub cube and is, to our knowledge, unprecedented. Cryo-electron microscopy confirms that the assemblies are held together by 120 S-Au-S staples between the protein oligomers, and exist in two chiral forms. The cage shows extreme chemical and thermal stability, yet it readily disassembles upon exposure to reducing agents. As well as gold, mercury(II) is also found to enable formation of the protein cage. This work establishes an approach for linking protein components into robust, higher-order structures, and expands the design space available for supramolecular assemblies to include previously unexplored geometries.
External linksPubMed:31068697 / Publisher's page
KeywordsRNA BINDING PROTEIN / TRAP; protein cage; gold binding; snub cube
MethodsEM (single particle)
Resolution3.7 - 5.9 A
Structure data

EMDB-4443:
Structure of left-handed protein cage consisting of 24 eleven-membered ring proteins held together by gold (I) bridges.

EMDB-4444:
Structure of right-handed protein cage consisting of 24 eleven-membered ring proteins held together by gold (I) bridges.

EMDB-6966:
Structure of protein cage consisting of 24 eleven-membered ring proteins induced by addition of gold nanoparticle (GNP)

PDB-6ib3:
Structure of left-handed protein cage consisting of 24 eleven-membered ring proteins held together by gold (I) bridges.

PDB-6ib4:
Structure of right-handed protein cage consisting of 24 eleven-membered ring proteins held together by gold (I) bridges.

Chemicals

ChemComp-AU:
GOLD IONGold

Source
  • geobacillus stearothermophilus (bacteria)

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