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

B MylemansT KillianL VandebroekLuc Van MeerveltJeremy R H TameT N Parac-VogtArnout R D Voet
Published in: Acta crystallographica. Section D, Structural biology (2021)
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.
Keyphrases
  • protein protein
  • amino acid
  • binding protein
  • single molecule
  • ionic liquid
  • single cell