3PG0
Crystal structure of designed 3-fold symmetric protein, ThreeFoil
Summary for 3PG0
| Entry DOI | 10.2210/pdb3pg0/pdb |
| Descriptor | ThreeFoil, 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, GLYCEROL, ... (5 entities in total) |
| Functional Keywords | symmetric design, beta-trefoil, engineered module, sugar binding, de novo protein |
| Biological source | Artificial gene |
| Total number of polymer chains | 1 |
| Total formula weight | 18896.30 |
| Authors | Lobsanov, Y.D.,Broom, A.,Howell, P.L.,Rose, D.R.,Meiering, E.M. (deposition date: 2010-10-29, release date: 2011-12-21, Last modification date: 2023-09-06) |
| Primary citation | Broom, A.,Doxey, A.C.,Lobsanov, Y.D.,Berthin, L.G.,Rose, D.R.,Howell, P.L.,McConkey, B.J.,Meiering, E.M. Modular evolution and the origins of symmetry: reconstruction of a three-fold symmetric globular protein. Structure, 20:161-171, 2012 Cited by PubMed Abstract: The high frequency of internal structural symmetry in common protein folds is presumed to reflect their evolutionary origins from the repetition and fusion of ancient peptide modules, but little is known about the primary sequence and physical determinants of this process. Unexpectedly, a sequence and structural analysis of symmetric subdomain modules within an abundant and ancient globular fold, the β-trefoil, reveals that modular evolution is not simply a relic of the ancient past, but is an ongoing and recurring mechanism for regenerating symmetry, having occurred independently in numerous existing β-trefoil proteins. We performed a computational reconstruction of a β-trefoil subdomain module and repeated it to form a newly three-fold symmetric globular protein, ThreeFoil. In addition to its near perfect structural identity between symmetric modules, ThreeFoil is highly soluble, performs multivalent carbohydrate binding, and has remarkably high thermal stability. These findings have far-reaching implications for understanding the evolution and design of proteins via subdomain modules. PubMed: 22178248DOI: 10.1016/j.str.2011.10.021 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.62 Å) |
Structure validation
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