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Crystal structures of Scone: pseudosymmetric folding of a symmetric designer protein
Author(s) -
Mylemans B.,
Killian T.,
Vandebroek L.,
Van Meervelt L.,
Tame J. R. H.,
Parac-Vogt T. N.,
Voet A. R. D.
Publication year - 2021
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.374
H-Index - 138
ISSN - 2059-7983
DOI - 10.1107/s2059798321005787
Subject(s) - crystallization , propeller , protein crystallization , folding (dsp implementation) , crystallography , protein folding , polyoxometalate , crystal structure , molecule , protein engineering , chemistry , engineering , mechanical engineering , biochemistry , marine engineering , organic chemistry , enzyme , catalysis
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.