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12 items found (0 items not approved), displaying 11 to 12.[First/Prev] 1, 2 [Next/Last]

Instruments / Technical Area	Publication Details	Published	Actions
I04-Macromolecular Crystallography	Computational design of symmetrical eight-bladed β-propeller proteins Hiroki Noguchi , Christine Addy , David Simoncini , Staf Wouters , Bram Mylemans , Luc Van Meervelt , Thomas Schiex , Kam Y. J. Zhang , Jeremy R. H. Tame , Arnout R. D. Voet Iucrj 6 DOI: 10.1107/S205225251801480X Open Access Show Abstract ▼ Abstract: β-Propeller proteins form one of the largest families of protein structures, with a pseudo-symmetrical fold made up of subdomains called blades. They are not only abundant but are also involved in a wide variety of cellular processes, often by acting as a platform for the assembly of protein complexes. WD40 proteins are a subfamily of propeller proteins with no intrinsic enzymatic activity, but their stable, modular architecture and versatile surface have allowed evolution to adapt them to many vital roles. By computationally reverse-engineering the duplication, fusion and diversification events in the evolutionary history of a WD40 protein, a perfectly symmetrical homologue called Tako8 was made. If two or four blades of Tako8 are expressed as single polypeptides, they do not self-assemble to complete the eight-bladed architecture, which may be owing to the closely spaced negative charges inside the ring. A different computational approach was employed to redesign Tako8 to create Ika8, a fourfold-symmetrical protein in which neighbouring blades carry compensating charges. Ika2 and Ika4, carrying two or four blades per subunit, respectively, were found to assemble spontaneously into a complete eight-bladed ring in solution. These artificial eight-bladed rings may find applications in bionanotechnology and as models to study the folding and evolution of WD40 proteins.	Nov 2018
I04-Macromolecular Crystallography	Design of tryptophan-containing mutants of the symmetrical Pizza protein for biophysical studies Hiroki Noguchi , Bram Mylemans , Elke De Zitter , Luc Van Meervelt , Jeremy R. H. Tame , Arnout Voet Biochemical And Biophysical Research Communications DOI: 10.1016/j.bbrc.2018.02.168 Diamond Proposal Number(s): [16692, 17167] Show Abstract ▼ Abstract: β-propeller proteins are highly symmetrical, being composed of a repeated motif with four anti-parallel β-sheets arranged around a central axis. Recently we designed the first completely symmetrical β-propeller protein, Pizza6, consisting of six identical tandem repeats. Pizza6 is expected to prove a useful building block for bionanotechnology, and also a tool to investigate the folding and evolution of β-propeller proteins. Folding studies are made difficult by the high stability and the lack of buried Trp residues to act as monitor fluorophores, so we have designed and characterized several Trp-containing Pizza6 derivatives. In total four proteins were designed, of which three could be purified and characterized. Crystal structures confirm these mutant proteins maintain the expected structure, and a clear redshift of Trp fluorescence emission could be observed upon denaturation. Among the derivative proteins, Pizza6-AYW appears to be the most suitable model protein for future folding/unfolding kinetics studies as it has a comparable stability as natural β-propeller proteins.	Feb 2018

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