6rvv

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

Loading... Status: waiting for Mol* initialization Structural highlights 6rvv is a 264 chain structure. This structure supersedes the now removed PDB entry 6ib3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: AU Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Symmetrical protein cages have evolved to fulfil diverse roles in nature, including compartmentalization and cargo delivery(1), 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(2,3). 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(i)-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. An ultra-stable gold-coordinated protein cage displaying reversible assembly.,Malay AD, Miyazaki N, Biela A, Chakraborti S, Majsterkiewicz K, Stupka I, Kaplan CS, Kowalczyk A, Piette BMAG, Hochberg GKA, Wu D, Wrobel TP, Fineberg A, Kushwah MS, Kelemen M, Vavpetic P, Pelicon P, Kukura P, Benesch JLP, Iwasaki K, Heddle JG Nature. 2019 May;569(7756):438-442. doi: 10.1038/s41586-019-1185-4. Epub 2019 May, 8. PMID:31068697 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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