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

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...

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Bibliographic Details
Published in:	Acta crystallographica. Section D, Biological crystallography. Vol. 77; no. 7; pp. 933 - 942
Main Authors:	Mylemans, B., Killian, T., Vandebroek, L., Van Meervelt, L., Tame, J. R. H., Parac-Vogt, T. N., Voet, A. R. D.
Format:	Journal Article
Language:	English
Published:	5 Abbey Square, Chester, Cheshire CH1 2HU, England International Union of Crystallography 01-07-2021 Wiley Subscription Services, Inc
Subjects:	Additives Computer applications Crystal structure Crystallization Crystallography Crystals Design polyoxometalates Polyoxometallates protein design Protein folding Proteins Scone symmetry β‐propeller
Online Access:	Get full text
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Summary:	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. Using computational protein design, a symmetric protein was designed; however, its crystal structures revealed a different pseudosymmetric architecture. Furthermore, one variant was only able to crystallize upon the addition of a polyoxometalate which links individual proteins in the crystal packing.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	2059-7983 0907-4449 2059-7983 1399-0047
DOI:	10.1107/S2059798321005787