4ow4

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

spinqualitylabelsall models 4ow4, resolution 2.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4ow4 is a 2 chain structure with sequence from Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.148Å Ligands: SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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 beta-trefoil protein by symmetric expansion of a beta-trefoil folding nucleus, previously identified by -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. Evolution and design of protein structure by folding nucleus symmetric expansion.,Longo LM, Kumru OS, Middaugh CR, Blaber M Structure. 2014 Oct 7;22(10):1377-84. doi: 10.1016/j.str.2014.08.008. Epub 2014, Sep 18. PMID:25242458 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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