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Instruments / Technical Area	Publication Details	Published	Actions
I04-Macromolecular Crystallography	Structural plasticity of a designer protein sheds light on β ‐propeller protein evolution Bram Mylemans , Ina Laier , Kenichi Kamata , Satoko Akashi , Hiroki Noguchi , Jeremy R. H. Tame , Arnout R. D. Voet The Febs Journal DOI: 10.1111/febs.15347 Diamond Proposal Number(s): [19190] Show Abstract ▼ Abstract: β‐propeller proteins are common in nature, where they are observed to adopt 4‐ to 10‐fold internal rotational pseudosymmetry. This size diversity can be explained by the evolutionary process of gene duplication and fusion. In this study we investigated a distorted β‐propeller protein, an apparent intermediate between two symmetries. From this template, we created a perfectly symmetric 9‐bladed β‐propeller named Cake, using computational design and ancestral sequence reconstruction. The designed repeat sequence was found to be capable of generating both 8‐fold and 9‐fold propellers which are highly stable. Cake variants with 2 to 10 identical copies of the repeat sequence were characterized by X‐ray crystallography and in solution. They were found to be highly stable, and to self‐assemble into 8‐ or 9‐ fold symmetrical propellers. These findings show that the β‐propeller fold allows sufficient structural plasticity to permit a given blade to assemble different forms, a transition from even to odd changes in blade number, and provide a potential explanation for the wide diversity of repeat numbers observed in natural propeller proteins.	Apr 2020

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I04-Macromolecular Crystallography

Structural plasticity of a designer protein sheds light on β ‐propeller protein evolution

Bram Mylemans , Ina Laier , Kenichi Kamata , Satoko Akashi , Hiroki Noguchi , Jeremy R. H. Tame , Arnout R. D. Voet

The Febs Journal

DOI: 10.1111/febs.15347

Diamond Proposal Number(s): [19190]

Show Abstract ▼

Apr 2020