4OW4

Beta-trefoil designed by folding nucleus symmetric expansion ("Phifoil")

Summary for 4OW4

• Entry DOI: 10.2210/pdb4ow4/pdb
• Descriptor: Beta-terfoil designed by folding nucleus symmetric expansion ("Phifoil"), SULFATE ION (3 entities in total)
• Functional Keywords: beta-trefoil, folding nucleus symmetric expansion, protein design, de novo, top-down symmetric deconstruction, de novo protein
• Biological source: synthetic construct
• Total number of polymer chains: 2
• Total formula weight: 27648.14

Authors

Blaber, M.,Longo, L.M. (deposition date: 2014-01-31, release date: 2014-12-17, Last modification date: 2023-12-27)

Primary citation

Longo, L.M.,Kumru, O.S.,Middaugh, C.R.,Blaber, M.
Evolution and design of protein structure by folding nucleus symmetric expansion.
Structure, 22:1377-1384, 2014

PubMed Abstract: Models of symmetric protein evolution typically invoke gene duplication and fusion events, in which repetition of a structural motif generates foldable, stable symmetric protein architecture. Success of such evolutionary processes suggests that the duplicated structural motif must be capable of nucleating protein folding. If correct, symmetric expansion of a folding nucleus sequence derived from an extant symmetric fold may be an elegant and computationally tractable solution to de novo protein design. We report the efficient de novo design of a β-trefoil protein by symmetric expansion of a β-trefoil folding nucleus, previously identified by ɸ-value analysis. The resulting protein, having exact sequence symmetry, exhibits superior folding properties compared to its naturally evolved progenitor-with the potential for redundant folding nuclei. In principle, folding nucleus symmetric expansion can be applied to any given symmetric protein fold (that is, nearly one-third of the known proteome) provided information of the folding nucleus is available.

PubMed: 25242458
DOI: 10.1016/j.str.2014.08.008

Experimental method

X-RAY DIFFRACTION (2.148 Å)