Article Metrics


Online attention

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

DOI: 10.1111/febs.15347 DOI Help

Authors: Bram Mylemans (KU Leuven) , Ina Laier (KU Leuven) , Kenichi Kamata (Yokohama City University) , Satoko Akashi (Yokohama City University) , Hiroki Noguchi (KU Leuven) , Jeremy R. H. Tame (Yokohama City University) , Arnout R. D. Voet (KU Leuven)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: The Febs Journal

State: Published (Approved)
Published: April 2020
Diamond Proposal Number(s): 19190

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.

Journal Keywords: Protein design; Protein crystallography; Protein evolution

Subject Areas: Biology and Bio-materials, Chemistry

Instruments: I04-Macromolecular Crystallography

Other Facilities: SOLEIL

Discipline Tags:

Technical Tags: