4OW4
Beta-trefoil designed by folding nucleus symmetric expansion ("Phifoil")
4OW4 の概要
| エントリーDOI | 10.2210/pdb4ow4/pdb |
| 分子名称 | Beta-terfoil designed by folding nucleus symmetric expansion ("Phifoil"), SULFATE ION (3 entities in total) |
| 機能のキーワード | beta-trefoil, folding nucleus symmetric expansion, protein design, de novo, top-down symmetric deconstruction, de novo protein |
| 由来する生物種 | synthetic construct |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 27648.14 |
| 構造登録者 | |
| 主引用文献 | 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 Cited by 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: 25242458DOI: 10.1016/j.str.2014.08.008 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.148 Å) |
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