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Crystal structures of Scone: pseudosymmetric folding of a symmetric designer protein

DOI: 10.1107/S2059798321005787 DOI Help

Authors: B. Mylemans (KU Leuven) , T. Killian (KU Leuven) , L. Vandebroek (KU Leuven) , L. Van Meervelt (KU Leuven) , J. R. H. Tame (Yokohama City University) , T. N. Parac-Vogt (KU Leuven) , A. R. D. Voet (KU Leuven)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section D Structural Biology , VOL 77

State: Published (Approved)
Published: July 2021
Diamond Proposal Number(s): 19190

Abstract: Recent years have seen an increase in the development of computational proteins, including symmetric ones. A ninefold-symmetric β-propeller protein named Cake has recently been developed. Here, attempts were made to further engineer this protein into a threefold-symmetric nine-bladed propeller using computational design. Two nine-bladed propeller proteins were designed, named Scone-E and Scone-R. Crystallography, however, revealed the structure of both designs to adopt an eightfold conformation with distorted termini, leading to a pseudo-symmetric protein. One of the proteins could only be crystallized upon the addition of a polyoxometalate, highlighting the usefulness of these molecules as crystallization additives.

Journal Keywords: protein design; polyoxometalates; β-propeller; symmetry; Scone

Subject Areas: Biology and Bio-materials

Instruments: I04-Macromolecular Crystallography

Added On: 30/06/2021 10:03

Discipline Tags:

Structural biology Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)